Chaperone protein DnaK
UniProt P0A6Y8 · gene dnaK · Escherichia coli (strain K12) · 638 residues
93evidence items
2mapped to a state
2states
8techniques
7sources
0conflicts
Coverage grid
Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).
| State | Basis | xray | nmr_structure | nmr_shifts | saxs_sans | force_spectroscopy | integrative | af_prediction | md | Total |
|---|---|---|---|---|---|---|---|---|---|---|
| ADP state, domains undocked DnaK-ADP-undocked | observed (one method) | · | proc 1 | · | · | · | · | · | · | 1 |
| ATP state, domains docked DnaK-ATP-docked | observed (one method) | proc 1 | · | · | · | · | · | · | · | 1 |
Unmapped evidence: 91 of 93 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 2 | 0 |
| DisProt | 1 | 0 |
| MDDB | 1 | 0 |
| RCSB PDB | 68 | 2 |
| SASBDB | 1 | 0 |
| SMASH-BIO | 19 | 0 |
Structure
Choose a state. Each model is badged observed or inferred; assumptions are one click away.
States and transitions
| State | Basis | Parent | Description |
|---|---|---|---|
| ADP state, domains undocked DnaK-ADP-undocked | observed | — | Nucleotide-binding and substrate-binding domains undocked, lid closed, ADP bound, as in 2KHO (NMR-RDC and X-ray). |
| ATP state, domains docked DnaK-ATP-docked | observed | — | Domains docked with the lid open, ATP bound, as in 4B9Q. |
No transitions recorded in this version (no rate or free-energy evidence has been curated yet).
Evidence
One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-13IQ-1 RCSB PDB | xray | resolution: 1.87 Å | in vitro · -173.15 °C · ligands A1DIB, SO4 E. coli DnaK bound to Telaprevir · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-13IU-1 RCSB PDB | xray | resolution: 1.87 Å | in vitro · -173.15 °C · ligands A1DF0 E. coli DnaK bound to peptide PA9 · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-13IV-1 RCSB PDB | xray | resolution: 3.23 Å | in vitro · -173.15 °C · ligands A1DFX E. coli DaK bound to peptide PA1, structure A · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-13JK-1 RCSB PDB | xray | resolution: 2.62 Å | in vitro · -173.15 °C · ligands A1DHT, IOD, SO4 E. coli DnaK bound to peptide PA5 · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-1BPR-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7 NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE · DNAK (chains A) | unmapped |
| EV-PDB-1DG4-1 RCSB PDB | nmr_structure | structure | in vitro · 29.85 °C · pH 6.8 NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM · DNAK (chains A) | unmapped |
| EV-PDB-1DKX-1 RCSB PDB | xray | resolution: 2 Å | in vitro THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 SELENOMETHIONYL CRYSTALS · SUBSTRATE BINDING DOMAIN OF DNAK (chains A) | unmapped |
| EV-PDB-1DKY-1 RCSB PDB | xray | resolution: 2.8 Å | in vitro THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS · DNAK (chains A,B) | unmapped |
| EV-PDB-1DKZ-1 RCSB PDB | xray | resolution: 2 Å | in vitro THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 NATIVE CRYSTALS · SUBSTRATE BINDING DOMAIN OF DNAK (chains A) | unmapped |
| EV-PDB-2KHO-1 RCSB PDB | nmr_structure | structure | in vitro · 26.85 °C · pH 7.2 NMR-RDC / XRAY structure of E. coli HSP70 (DNAK) chaperone (1-605) complexed with ADP and substrate · Heat shock protein 70 (chains A) | ADP state, domains undocked · curator:draft (unreviewed) · high Full-length DnaK with ADP and substrate, NMR-RDC refined. |
| EV-PDB-3DPO-1 RCSB PDB | xray | resolution: 2.1 Å | in vitro · -173.15 °C · pH 5 · ligands SO4 Crystal structure of the substrate binding domain of E. coli DnaK in complex with a short pyrrhocoricin-derived inhibitor peptide · Chaperone protein dnaK (chains A,B) | unmapped |
| EV-PDB-3DPP-1 RCSB PDB | xray | resolution: 2.5 Å | in vitro · 19.85 °C · pH 5 · ligands SO4 Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form A) · Chaperone protein dnaK (chains A,B) | unmapped |
| EV-PDB-3DPQ-1 RCSB PDB | xray | resolution: 2.6 Å | in vitro · 19.85 °C · pH 5 · ligands SO4 Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form B) · Chaperone protein dnaK (chains A,B,E,F) | unmapped |
| EV-PDB-4B9Q-1 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · pH 7.6 · ligands ATP, MG Open conformation of ATP-bound Hsp70 homolog DnaK · CHAPERONE PROTEIN DNAK (chains A,B,C,D) | ATP state, domains docked · curator:draft (unreviewed) · high Title: open conformation of ATP-bound DnaK. |
| EV-PDB-4E81-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 6 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with a short apidaecin peptide · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4EZN-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · pH 5 Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4EZO-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 4 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-39 (residues 1 to 15) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4EZQ-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 9 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the C-terminal part of pyrrhocoricin (residues 12 to 20) · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4EZR-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 9 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the C-terminal part of drosocin (residues 12 to 19) · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4EZS-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 8 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with metchnikowin (residues 20 to 26) · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4EZU-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 8 Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-bombesin in space group I222 · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4EZV-1 RCSB PDB | xray | resolution: 2.1 Å | in vitro · -173.15 °C · pH 8 Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-bombesin in space group P21212 · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4EZW-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · pH 4.1 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide NRLLLTG · Chaperone protein DnaK (chains A,B,C,D) | unmapped |
| EV-PDB-4EZX-1 RCSB PDB | xray | resolution: 1.7 Å | in vitro · -173.15 °C · pH 4 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide NRLMLTG · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4EZZ-1 RCSB PDB | xray | resolution: 2.05 Å | in vitro · -173.15 °C · pH 9 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide ELPLVKI · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4F00-1 RCSB PDB | xray | resolution: 1.95 Å | in vitro · -173.15 °C · pH 4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with an apidaecin fragment from the bumblebee (residues 3 to 11) · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4F01-1 RCSB PDB | xray | resolution: 1.4 Å | in vitro · -173.15 °C · pH 6.4 Crystal structure of an artificial dimeric DnaK complex · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4HY9-1 RCSB PDB | xray | resolution: 1.55 Å | in vitro · -173.15 °C · pH 4.1 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZZ (residues 1 to 11) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4HYB-1 RCSB PDB | xray | resolution: 1.7 Å | in vitro · -173.15 °C · pH 5 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with pyrrhocoricin_LYZI (residues 1 to 10) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4JNE-1 RCSB PDB | xray | resolution: 1.96 Å | in vitro · -173.15 °C · pH 7.5 · ligands ATP, GOL, MG, SO4 Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP · Hsp70 CHAPERONE DnaK (chains A,B) | unmapped |
| EV-PDB-4JWD-1 RCSB PDB | xray | resolution: 1.95 Å | in vitro · -173.15 °C · pH 4.4 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with bovine Bac7(15-28) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4JWE-1 RCSB PDB | xray | resolution: 1.95 Å | in vitro · -173.15 °C · pH 5 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep Bac7(1-21) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4JWI-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 4.4 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with sheep Bac7(35-43) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4R5G-1 RCSB PDB | xray | resolution: 3.4501 Å | in vitro · -173.15 °C · pH 5.5 · ligands 3JE Crystal structure of the DnaK C-terminus with the inhibitor PET-16 · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4R5I-1 RCSB PDB | xray | resolution: 1.9702 Å | in vitro · -173.15 °C · pH 5.5 · ligands PO4, SO4 Crystal structure of the DnaK C-terminus with the substrate peptide NRLLLTG · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4R5K-1 RCSB PDB | xray | resolution: 1.7469 Å | in vitro · -173.15 °C · ligands CA, SO4 Crystal structure of the DnaK C-terminus (Dnak-SBD-B) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4R5L-1 RCSB PDB | xray | resolution: 2.9701 Å | in vitro · -173.15 °C · pH 5.5 · ligands CA, PO4, SO4 Crystal structure of the DnaK C-terminus (Dnak-SBD-C) · Chaperone protein DnaK (chains A,B,C,D) | unmapped |
| EV-PDB-5NRO-1 RCSB PDB | xray | resolution: 3.25 Å | in vitro · -173.15 °C · ligands ATP, MG Structure of full-length DnaK with bound J-domain · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4R5J-1 RCSB PDB | xray | resolution: 2.361 Å | in vitro · -173.15 °C · ligands CA, PO4 Crystal structure of the DnaK C-terminus (Dnak-SBD-A) · Chaperone protein DnaK (chains A,B,C,D) | unmapped |
| EV-PDB-4JWC-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · pH 4.4 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with bovine Bac7(1-16) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4JNF-1 RCSB PDB | xray | resolution: 1.621 Å | in vitro · -173.15 °C · pH 8.5 Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP · Hsp70 CHAPERONE DnaK (chains A) | unmapped |
| EV-PDB-4JN4-1 RCSB PDB | xray | resolution: 2.3 Å | in vitro · -173.15 °C · pH 7.5 · ligands ATP, GOL, MG, SO4 Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-4EZY-1 RCSB PDB | xray | resolution: 1.85 Å | in vitro · -173.15 °C · pH 6 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide NRLILTG · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4EZT-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 7 Crystal structure of the substrate binding domain of E.coli DnaK in complex with heliocin (residues 14 to 21) · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-4EZP-1 RCSB PDB | xray | resolution: 1.65 Å | in vitro · -173.15 °C · pH 5 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with A3-APO(residues 1 to 20) · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-3QNJ-1 RCSB PDB | xray | resolution: 2.28 Å | in vitro · -173.15 °C · pH 4 · ligands SO4 Crystal structure of the substrate binding domain of E.coli DnaK in complex with the antimicrobial peptide oncocin · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-2BPR-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7 NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, 25 STRUCTURES · DNAK (chains A) | unmapped |
| EV-PDB-1Q5L-1 RCSB PDB | nmr_structure | structure | in vitro · 29.85 °C · pH 7.4 NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG · Chaperone protein dnaK (chains A) | unmapped |
| EV-PDB-1DKG-2 RCSB PDB | xray | resolution: 2.8 Å | in vitro · -173.15 °C · pH 4.6 CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK · MOLECULAR CHAPERONE DNAK (chains D) | unmapped |
| EV-PDB-13JG-1 RCSB PDB | xray | resolution: 1.52 Å | in vitro · -173.15 °C · ligands A1DFX, SO4 E. coli DnaK bound to peptide PA1, structure B · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-5OOW-1 RCSB PDB | xray | resolution: 2.9 Å | in vitro · -173.15 °C · pH 7 · ligands ACP Crystal structure of lobe II from the nucleotide binding domain of DnaK in complex with AMPPCP · Chaperone protein DnaK (chains A,B) | unmapped |
| EV-PDB-7JMM-1 RCSB PDB | xray | resolution: 2.56 Å | in vitro · -173.15 °C · pH 7 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RAKNIILLSR · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7JN8-1 RCSB PDB | xray | resolution: 3.09 Å | in vitro · -173.15 °C · pH 7 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RGNTLVIVSR · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7JNE-1 RCSB PDB | xray | resolution: 2.54 Å | in vitro · -173.15 °C · pH 7 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RGSQLRIASR · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7KO2-1 RCSB PDB | xray | resolution: 2.64 Å | in vitro · -173.15 °C · ligands ATP, MG, SO4 Restraining state of near full-length Hsp70 DnaK · Chaperone protein DnaK (chains A,B,C,D) | unmapped |
| EV-PDB-7KRT-1 RCSB PDB | xray | resolution: 2.79 Å | in vitro · -173.15 °C · ligands ATP, MG Restraining state of a truncated Hsp70 DnaK · Chaperone protein DnaK (chains A,B,C,D) | unmapped |
| EV-PDB-7KRV-1 RCSB PDB | xray | resolution: 1.92 Å | in vitro · -173.15 °C · ligands 6LN, ATP, MG, SO4 Stimulating state of disulfide-bridged Hsp70 DnaK · Chaperone protein DnaK fused with substrate peptide (chains A,B) | unmapped |
| EV-PDB-7KRW-1 RCSB PDB | xray | resolution: 7.7 Å | in vitro · -173.15 °C · ligands ATP Stimulating state of near full-length Hsp70 DnaK fused with a substrate peptide · Chaperone protein DnaK fused with substrate peptide (chains A,B,C,D) | unmapped |
| EV-PDB-7KZI-1 RCSB PDB | xray | resolution: 2.82 Å | in vitro · -173.15 °C · ligands ATP, CL, MG, SO4 Intermediate state (QQQ) of near full-length DnaK alternatively fused with a substrate peptide · Chaperone protein DnaK fused with substrate peptide,Chaperone protein DnaK fused with substrate peptide (chains A,B) | unmapped |
| EV-PDB-7KZU-1 RCSB PDB | xray | resolution: 2.15 Å | in vitro · -173.15 °C · ligands ATP, GOL, MG, SO4 Quasi-intermediate state (Q) of a truncated Hsp70 DnaK fused with a substrate peptide · Chaperone protein DnaK fused with substrate peptide,Chaperone protein DnaK fused with substrate peptide (chains A) | unmapped |
| EV-PDB-7N6J-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 7 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RKQSTIALALLPLLFTPRR · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7N6L-1 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · pH 7 · ligands GOL, SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide EANQQKPLLGLFADG · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7N6M-1 RCSB PDB | xray | resolution: 1.82 Å | in vitro · -173.15 °C · pH 7 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RQKPLLGLSR · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7RAX-1 RCSB PDB | xray | resolution: 1.41 Å | in vitro · -173.15 °C · ligands ATP, GOL, K, MG, NA ATP-binding state of the nucleotide-binding domain of Hsp70 DnaK mutant T199A · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-9A2I-1 RCSB PDB | integrative | structure | in vitro Model of E. coli DnaK by in-cell photo-crosslinking MS and deep learning · P0A6Y8 (chains A) | unmapped |
| EV-PDB-7N6K-1 RCSB PDB | xray | resolution: 2.55 Å | in vitro · -173.15 °C · pH 6.9 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RALALLPLSR · Chaperone protein DnaK (chains A) | unmapped |
| EV-PDB-7KRU-1 RCSB PDB | xray | resolution: 1.82 Å | in vitro · -173.15 °C · ligands ATP, GOL, MG, PDO, SO4 Stimulating state of a truncated Hsp70 DnaK fused with a substrate peptide · Chaperone protein DnaK fused with substrate peptide (chains A,B) | unmapped |
| EV-PDB-7JN9-1 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · pH 7 · ligands SO4 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide QEHTGSQLRIAAYGP · Chaperone protein DnaK (chains A) | unmapped |
| EV-BMRB-27392 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 7.2 E.Coli DnaK Nucleotide Binding Domain · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-51802 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 7 Backbone assignment of DnaK C-terminal alpha-helical lid with C-IDR · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-SASBDB-SASDXF5 SASBDB | saxs_sans | radius_of_gyration: 3.828 nm ± 0.108 | in vitro · 25 °C · pH 8 · ligands partner: Heme ligase Recombinant expression and purification of Plasmodium heme detoxification protein in E. coli: Challenges and discoveries. · Chaperone protein DnaK with Heme ligase | unmapped |
| EV-DISPROT-DP02985r001 DisProt | nmr_shifts | disorder_region: 33 residues | in vitro DisProt DP02985: disorder, residues 606-638 · residues 606-638; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-AFDB-AF-P0A6Y8-F1 AlphaFold DB | af_prediction | plddt: 92.25 pLDDT | in silico AlphaFold DB prediction AF-P0A6Y8-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-638 | unmapped |
| EV-MDDB-A004W MDDB | md | trajectory: 10 ns | in silico · 26.85 °C MoDEL 1BPR · start 1BPR; Amber Parm99 | unmapped |
| EV-SMASH-SMFS-000620 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycle. · Hsp70 chaperone (DnaK); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001131 SMASH-BIO | force_spectroscopy | study_record | in vitro Effect of temperature and nucleotide on the binding of BiP chaperone to a protein substrate. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001399 SMASH-BIO | force_spectroscopy | study_record | in vitro Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: receptor_ligand_adhesion, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001479 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct Observation of the Mechanical Role of Bacterial Chaperones in Protein Folding. · Hsp70 chaperone (DnaK); magnetic tweezers; experiment class: force_generation_motor, rheology_cell, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001481 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct observation of Hsp90-induced compaction in a protein chain. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: nucleic_acid_protein_interaction, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001482-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 11 pN | in vitro · pH 7.4 Direct observation of chaperone-modulated talin mechanics with single-molecule resolution. · Hsp70 chaperone (DnaK); magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001483 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct observation of chemo-mechanical coupling in DnaK by single-molecule force experiments. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001885 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct observation of Hsp90-induced compaction in a protein chain · Hsp70 chaperone (DnaK); optical tweezers; experiment class: nucleic_acid_protein_interaction, receptor_ligand_adhesion, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001975 SMASH-BIO | force_spectroscopy | study_record | in vitro Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002102-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 6 pN | in vitro Real Time Observation of Chaperone-modulated Talin Mechanics Under Single Molecule Resolution · Hsp70 chaperone (DnaK); magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002103-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 6 pN | in vitro Real time observation of chaperone-modulated talin mechanics with single molecule resolution · Hsp70 chaperone (DnaK); magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002306 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct observation of the mechanical role of bacterial chaperones in protein folding · Hsp70 chaperone (DnaK); magnetic tweezers; experiment class: force_generation_motor, rheology_cell, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002982 SMASH-BIO | force_spectroscopy | study_record | in vitro A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003301 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003342 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 The force-dependent mechanism of DnaK-mediated mechanical folding. · Hsp70 chaperone (DnaK); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003693 SMASH-BIO | force_spectroscopy | study_record | in vitro Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003817 SMASH-BIO | force_spectroscopy | study_record | in vitro Alternative modes of client binding enable functional plasticity of Hsp70. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004314 SMASH-BIO | force_spectroscopy | study_record | in vitro Nucleotides regulate the mechanical hierarchy between subdomains of the nucleotide binding domain of the Hsp70 chaperone DnaK. · Hsp70 chaperone (DnaK); optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006953 SMASH-BIO | force_spectroscopy | study_record | in vitro Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements. · Hsp70 chaperone (DnaK); afm smfs; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
Conflicts
No conflicts found among comparable evidence.
92 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.
Downloads
- Protein bundle (JSON)
- DnaK-ADP-undocked-cif (mmCIF, observed)
- DnaK-ADP-undocked-pdb (PDB, observed)
- DnaK-ATP-docked-cif (mmCIF, observed)
- DnaK-ATP-docked-pdb (PDB, observed)
- Curation file (YAML)