DNA helicase II
UniProt P03018 · gene uvrD · Escherichia coli (strain K12) · 720 residues
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 | force_spectroscopy | af_prediction | Total |
|---|---|---|---|---|---|---|---|
| No states defined yet. | |||||||
Unmapped evidence: 18 of 18 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 1 | 0 |
| RCSB PDB | 7 | 0 |
| SMASH-BIO | 9 | 0 |
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.
| State | Basis | Parent | Description |
|---|
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-2IS1-3 RCSB PDB | xray | resolution: 2.9 Å | in vitro · -173.15 °C · pH 7 · ligands GOL, HG, SO4 Crystal structure of UvrD-DNA-SO4 complex · DNA helicase II (chains A,B) | unmapped |
| EV-PDB-2IS2-2 RCSB PDB | xray | resolution: 3 Å | in vitro · -173.15 °C · pH 7 · ligands FMT, GOL Crystal structure of UvrD-DNA binary complex · DNA helicase II (chains A,B) | unmapped |
| EV-PDB-2IS6-2 RCSB PDB | xray | resolution: 2.2 Å | in vitro · -173.15 °C · pH 7 · ligands ADP, GOL, MG, MGF Crystal structure of UvrD-DNA-ADPMgF3 ternary complex · DNA helicase II (chains A,B) | unmapped |
| EV-PDB-7EGS-2 RCSB PDB | xray | resolution: 1.7 Å | in vitro · -173.15 °C · ligands GOL The crystal structure of lobe domain of E. coli RNA polymerase complexed with the C-terminal domain of UvrD · DNA helicase II (chains B) | unmapped |
| EV-PDB-6YI2-1 RCSB PDB | nmr_structure | structure | in vitro · 36.85 °C · pH 6.5 UvrD helicase RNA polymerase interactions are governed by UvrDs carboxy terminal Tudor domain. · DNA helicase (chains A) | unmapped |
| EV-PDB-3LFU-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -143.15 °C · pH 9.1 · ligands SO4 Crystal Structure of E. coli UvrD · DNA helicase II (chains A) | unmapped |
| EV-PDB-2IS4-2 RCSB PDB | xray | resolution: 2.6 Å | in vitro · -173.15 °C · pH 7 · ligands ANP, MG Crystal structure of UvrD-DNA-ADPNP ternary complex · DNA helicase II (chains A,B) | unmapped |
| EV-BMRB-50218 BMRB | nmr_shifts | chemical_shift | in vitro · 36.85 °C · pH 6.5 UvrD_CTD · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-AFDB-AF-P03018-F1 AlphaFold DB | af_prediction | plddt: 87.44 pLDDT | in silico AlphaFold DB prediction AF-P03018-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-720 | unmapped |
| EV-SMASH-SMFS-001978 SMASH-BIO | force_spectroscopy | study_record | in vitro Kinetic and structural mechanism for DNA unwinding by a non-hexameric helicase · UvrD helicase; optical tweezers; experiment class: force_generation_motor, nucleic_acid_protein_interaction, translation_transcription_replication, unfolding_nucleic_acid, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001979 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8 Kinetic and structural mechanism for DNA unwinding by a non-hexameric helicase. · UvrD helicase; optical tweezers; experiment class: force_generation_motor, nucleic_acid_protein_interaction, translation_transcription_replication, unfolding_nucleic_acid, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003461 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct Visualization of Helicase Dynamics Using Fluorescence Localization and Optical Trapping. · UvrD helicase; optical tweezers; experiment class: force_generation_motor, nucleic_acid_protein_interaction, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-003650 SMASH-BIO | force_spectroscopy | study_record | in vitro Probing Single Helicase Dynamics on Long Nucleic Acids Through Fluorescence-Force Measurement. · UvrD helicase; optical tweezers; experiment class: force_generation_motor, nucleic_acid_protein_interaction, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-004341 SMASH-BIO | force_spectroscopy | study_record | in vitro Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme. · UvrD helicase; optical tweezers; experiment class: nucleic_acid_protein_interaction, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-004842 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8.3 Direct imaging of single UvrD helicase dynamics on long single-stranded DNA. · UvrD helicase; optical tweezers; experiment class: force_generation_motor, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-006352-r0 SMASH-BIO | force_spectroscopy | velocity: 150 nt/s | in vitro Impediment of E. coli UvrD by DNA-destabilizing force reveals a strained-inchworm mechanism of DNA unwinding. · UvrD helicase; magnetic tweezers; experiment class: force_generation_motor, translation_transcription_replication, unfolding_nucleic_acid | unmapped |
| EV-SMASH-SMFS-006767 SMASH-BIO | force_spectroscopy | study_record | in vitro DNA mechanics as a tool to probe helicase and translocase activity. · UvrD helicase; afm smfs; experiment class: chromatin_mechanics, force_generation_motor, nucleic_acid_mechanics, nucleic_acid_protein_interaction, translation_transcription_replication, unfolding_nucleic_acid, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007199 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule assay reveals strand switching and enhanced processivity of UvrD. · UvrD helicase; force spectroscopy unspecified; experiment class: force_generation_motor, nucleic_acid_protein_interaction, translation_transcription_replication | unmapped |
Conflicts
No conflicts found among comparable evidence.
18 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.