Ankyrin-1

UniProt P16157 · gene ANK1 · Homo sapiens · 1881 residues

37evidence items
0mapped to a state
0states
6techniques
4sources
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).

StateBasisxraycryoemnmr_structurenmr_shiftsforce_spectroscopyaf_predictionTotal
No states defined yet.

Unmapped evidence: 37 of 37 items. Mappings come from curator assignments and curated rules; see About for how rules work.

Sources

SourceEvidenceMapped
AlphaFold DB10
BMRB10
RCSB PDB210
SMASH-BIO140

Structure

No state models are exported for this protein yet. Observed states export the representative PDB entry; inferred states need fitted models, not yet built.

States and transitions

No states defined.

StateBasisParentDescription

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.

EvidenceTechniqueObservableConditionsMapped to state
EV-PDB-1N11-1
RCSB PDB
xrayresolution: 2.7 Åin vitro · -173.15 °C · pH 7.5 · ligands BR, CL
D34 REGION OF HUMAN ANKYRIN-R AND LINKER · Ankyrin (chains A)
unmapped
EV-PDB-2YQF-1
RCSB PDB
nmr_structurestructurein vitro · 24.85 °C · pH 7
Solution structure of the death domain of Ankyrin-1 · Ankyrin-1 (chains A)
unmapped
EV-PDB-2YVI-1
RCSB PDB
xrayresolution: 1.92 Åin vitro · -173.15 °C · pH 8.5 · ligands GOL
Crystal structure of a death domain of human ankryn protein · Ankyrin-1 (chains A)
unmapped
EV-PDB-3KBT-2
RCSB PDB
xrayresolution: 2.75 Åin vitro · -173.15 °C · pH 6.5
Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK) · Ankyrin-1 (chains C,D)
unmapped
EV-PDB-3KBU-2
RCSB PDB
xrayresolution: 2.75 Åin vitro · -173.15 °C · pH 6.5 · ligands HG
Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK), EMTS derivative · Ankyrin-1 (chains C,D)
unmapped
EV-PDB-3UD1-1
RCSB PDB
xrayresolution: 2 Åin vitro · -173.15 °C · pH 7 · ligands EOH
Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin · Ankyrin-1 (chains A,B,C)
unmapped
EV-PDB-7TW3-3
RCSB PDB
cryoemresolution: 4.4 Åin vitro
Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cell · Ankyrin-1 (chains G)
unmapped
EV-PDB-7UZU-1
RCSB PDB
cryoemresolution: 2.3 Åin vitro
Ankyrin-1 (N-terminal region of membrane binding domain, local refinement from consensus reconstruction; bound to N-terminal peptide from band 3) · Ankyrin-1 (chains A)
unmapped
EV-PDB-8CS9-1
RCSB PDB
cryoemresolution: 2.74 Åin vitro · ligands AJP, CLR, NAG, PIO, branched: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A)
unmapped
EV-PDB-8CSL-1
RCSB PDB
cryoemresolution: 25 Åin vitro
Sub-tomogram averaging of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A)
unmapped
EV-PDB-8CTE-1
RCSB PDB
cryoemresolution: 2.9 Åin vitro · ligands AJP, CLR, NAG, PIO
Class 2 of erythrocyte ankyrin-1 complex (Composite map) · Ankyrin-1 (chains A)
unmapped
EV-PDB-8CSV-1
RCSB PDB
cryoemresolution: 2.7 Åin vitro
Local refinement of Anykyrin-1 (N-terminal half of membrane binding domain) in Class 2 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A)
unmapped
EV-PDB-7V0X-1
RCSB PDB
cryoemresolution: 3 Åin vitro
Local refinement of ankyrin-1 (C-terminal half), class 1 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains J)
unmapped
EV-PDB-7V0S-3
RCSB PDB
cryoemresolution: 2.5 Åin vitro · ligands AJP, CLR
Local refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains J)
unmapped
EV-PDB-7V0M-1
RCSB PDB
cryoemresolution: 2.7 Åin vitro
Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex · Ankyrin-1 (chains A)
unmapped
EV-PDB-7V0K-3
RCSB PDB
cryoemresolution: 2.4 Åin vitro · ligands AJP, CLR, NAG, PIO, PLC
Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map) · Ankyrin-1 (chains H)
unmapped
EV-PDB-7UZQ-3
RCSB PDB
cryoemresolution: 2.17 Åin vitro · ligands AJP, CLR
Local refinement of RhAG-RhCE-ANK1(AR1-5), from consensus refinement of all classes · Ankyrin-1 (chains J)
unmapped
EV-PDB-7TW6-3
RCSB PDB
cryoemresolution: 5.6 Åin vitro
Cryo-EM structure of human ankyrin complex (B4P1A1) from red blood cell · Ankyrin-1 (chains G)
unmapped
EV-PDB-7TW5-3
RCSB PDB
cryoemresolution: 5.7 Åin vitro
Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell · Ankyrin-1 (chains G,H)
unmapped
EV-PDB-3UD2-1
RCSB PDB
xrayresolution: 2.21 Åin vitro · -173.15 °C · pH 7 · ligands CL, EOH, NA
Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin · Ankyrin-1 (chains A,B,C)
unmapped
EV-PDB-3F59-1
RCSB PDB
xrayresolution: 2 Åin vitro · -173.15 °C · pH 6.5 · ligands BR
Crystal structure of ZU5-ANK, the spectrin binding region of human erythroid ankyrin · Ankyrin-1 (chains A,B,C,D)
unmapped
EV-BMRB-11390
BMRB
nmr_shiftschemical_shiftin vitro · 24.85 °C · pH 7
Solution structure of the death domain of Ankyrin-1 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts
unmapped
EV-AFDB-AF-P16157-F1
AlphaFold DB
af_predictionplddt: 69.75 pLDDTin silico
AlphaFold DB prediction AF-P16157-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-1881
unmapped
EV-SMASH-SMFS-000217
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 8.5
Nonlinear stiffness of NompC gating spring and its implication in mechanotransduction. · Ankyrin repeats; optical tweezers; experiment class: unfolding_protein
unmapped
EV-SMASH-SMFS-000872-r0
SMASH-BIO
force_spectroscopymolecular_stiffness: 0.7 pN/nmin vitro
Nonlinear compliance of NompC gating spring and its implication in mechanotransduction · Ankyrin repeats; optical tweezers; experiment class: unfolding_protein
unmapped
EV-SMASH-SMFS-001694
SMASH-BIO
force_spectroscopystudy_recordin vitro
Reconstruction of mechanical unfolding and refolding pathways of proteins with atomic force spectroscopy and computer simulations. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein
unmapped
EV-SMASH-SMFS-002527-r0
SMASH-BIO
force_spectroscopypersistence_length: 0.35 nmin vitro · pH 7.2
Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP. · Ankyrin repeats; afm smfs; experiment class: rheology_cell, unfolding_protein
unmapped
EV-SMASH-SMFS-002527-r1
SMASH-BIO
force_spectroscopycontour_length: 39 nmin vitro · pH 7.2
Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP. · Ankyrin repeats; afm smfs; experiment class: rheology_cell, unfolding_protein
unmapped
EV-SMASH-SMFS-004379-r0
SMASH-BIO
force_spectroscopyunbinding_force: 30 pNin vitro
Spectrin-ankyrin interaction mechanics: A key force balance factor in the red blood cell membrane skeleton. · Ankyrin repeats; afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell
unmapped
EV-SMASH-SMFS-004480
SMASH-BIO
force_spectroscopystudy_recordin vitro
Capturing the mechanical unfolding pathway of a large protein with coiled-coil probes. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein
unmapped
EV-SMASH-SMFS-005095
SMASH-BIO
force_spectroscopystudy_recordin vitro
A hot-spot motif characterizes the interface between a designed ankyrin-repeat protein and its target ligand. · Ankyrin repeats; force spectroscopy unspecified; experiment class: membrane_mechanics, receptor_ligand_adhesion
unmapped
EV-SMASH-SMFS-005201
SMASH-BIO
force_spectroscopystudy_recordin vitro
Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding. · Ankyrin repeats; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell
unmapped
EV-SMASH-SMFS-005244-r0
SMASH-BIO
force_spectroscopyunfolding_force: 30 pNin vitro
Mechanical anisotropy of ankyrin repeats. · Ankyrin repeats; afm smfs; experiment class: rheology_cell, unfolding_protein
unmapped
EV-SMASH-SMFS-005261
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7.4
Mutation of conserved histidines alters tertiary structure and nanomechanics of consensus ankyrin repeats. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein
unmapped
EV-SMASH-SMFS-005788
SMASH-BIO
force_spectroscopystudy_recordin vitro
Fast and forceful refolding of stretched alpha-helical solenoid proteins. · Ankyrin repeats; afm smfs; experiment class: unfolding_protein
unmapped
EV-SMASH-SMFS-005807
SMASH-BIO
force_spectroscopystudy_recordin vitro
Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations. · Ankyrin repeats; force spectroscopy unspecified; experiment class: translation_transcription_replication, unfolding_protein
unmapped
EV-SMASH-SMFS-007546
SMASH-BIO
force_spectroscopystudy_recordin vitro
Elasticity of the red cell membrane and its relation to hemolytic disorders: an optical tweezers study. · Ankyrin repeats; optical tweezers; experiment class: force_generation_motor, rheology_cell, unfolding_protein
unmapped

Conflicts

No conflicts found among comparable evidence.

37 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.

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