Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01714
- Gene
- AHE46982.1 uvrD
- Status
- annotated
- Amino acids
- 720
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 95.972
- DEG E-value
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 87.83
Selected Druggability evidence
AlphaFold / UniProt modelSelected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
13- GO:0006268 OBSOLETE. The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication.
- GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
- GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0033202 A protein complex that possesses DNA helicase activity.
- GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis.
- GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
- GO:0042802 Binding to an identical protein or proteins.
- GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
- GO:0000725 A DNA repair process that involves the exchange, reciprocal or nonreciprocal, of genetic material between the broken DNA molecule and a homologous DNA region.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 281 | 636 | Gene3D | G3DSA:3.40.50.300 | - |
| 281 | 636 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 8 | 286 | ProSiteProfiles | PS51198 | UvrD-like DNA helicase ATP-binding domain profile. |
| 8 | 286 | InterPro | IPR014016 | UvrD-like helicase, ATP-binding domain |
| 114 | 187 | FunFam | G3DSA:1.10.10.160:FF:000002 | DNA helicase |
| 114 | 187 | Gene3D | G3DSA:1.10.10.160 | - |
| 114 | 187 | InterPro | IPR013986 | DExx box DNA helicase domain superfamily |
| 280 | 383 | FunFam | G3DSA:3.40.50.300:FF:001201 | ATP-dependent DNA helicase UvrD2 |
| 287 | 564 | ProSiteProfiles | PS51217 | UvrD-like DNA helicase C-terminal domain profile. |
| 287 | 564 | InterPro | IPR014017 | UvrD-like DNA helicase, C-terminal |
| 10 | 271 | Pfam | PF00580 | UvrD/REP helicase N-terminal domain |
| 10 | 271 | InterPro | IPR014016 | UvrD-like helicase, ATP-binding domain |
| 7 | 642 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 7 | 642 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 6 | 718 | NCBIfam | TIGR01075 | DNA helicase UvrD |
| 6 | 718 | InterPro | IPR005753 | DNA helicase, ATP-dependent, UvrD type |
| 9 | 647 | PANTHER | PTHR11070 | UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER |
| 9 | 647 | InterPro | IPR000212 | DNA helicase, UvrD/REP type |
| 10 | 274 | Gene3D | G3DSA:3.40.50.300 | - |
| 10 | 274 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 285 | 614 | CDD | cd18807 | SF1_C_UvrD |
| 382 | 538 | FunFam | G3DSA:1.10.486.10:FF:000001 | DNA helicase |
| 382 | 538 | Gene3D | G3DSA:1.10.486.10 | PCRA; domain 4 |
| 277 | 616 | Pfam | PF13361 | UvrD-like helicase C-terminal domain |
| 277 | 616 | InterPro | IPR014017 | UvrD-like DNA helicase, C-terminal |
| 11 | 283 | CDD | cd17932 | DEXQc_UvrD |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GGJ9
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01714
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 8.6 | 0.46 | ||||||
| 2 | 7.85 | 0.416 | ||||||
| 3 | 4.02 | 0.16 | ||||||
| 4 | 1.92 | 0.039 | ||||||
| 5 | 1.9 | 0.038 |
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 29 | 0.446 | ||||||
| 16 | 0.389 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 7.15 | 0.372 | ||||||
| 2 | 6.04 | 0.298 | ||||||
| 3 | 3.99 | 0.159 | ||||||
| 4 | 2.98 | 0.097 | ||||||
| 5 | 2.01 | 0.044 |
Ligand evidence
Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC12360002 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC12360703 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC12503599 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC16546165 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…
|
| ZINC31977053 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…
|
| ZINC4806433 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC53683898 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC8586019 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…
|
| ZINC8586020 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC8586021 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…
|
| ZINC8586022 | 0.810 | 427.2 Da LogP -1.75 TPSA 232.6 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…
|
| ZINC13518964 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…
|
| ZINC1532515 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…
|
| ZINC1571045 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…
|
| ZINC1842158 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…
|
| ZINC2046931 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…
|
| ZINC2126310 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…
|
| ZINC3201891 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…
|
| ZINC3201893 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…
|
| ZINC3830180 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…
|
| ZINC3860156 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…
|
| ZINC3977897 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…
|
| ZINC4806442 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…
|
| ZINC8613167 | 0.741 | 347.2 Da LogP -1.86 TPSA 186.1 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…
|
| ZINC4096224 | 0.729 | 346.2 Da LogP -1.90 TPSA 191.9 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…
|
| ZINC12503850 | 0.726 | 427.3 Da LogP -2.04 TPSA 229.4 | 1 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…
|
| ZINC141161066 | 0.726 | 427.3 Da LogP -2.04 TPSA 229.4 | 1 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…
|
| ZINC141163786 | 0.726 | 427.3 Da LogP -2.04 TPSA 229.4 | 1 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…
|
| ZINC4228246 | 0.726 | 427.3 Da LogP -2.04 TPSA 229.4 | 1 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…
|
| ZINC105372833 | 0.712 | 345.3 Da LogP -1.93 TPSA 197.6 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…
|
| ZINC105372837 | 0.712 | 345.3 Da LogP -1.93 TPSA 197.6 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…
|
| ZINC17107643 | 0.712 | 345.3 Da LogP -1.93 TPSA 197.6 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…
|
| ZINC204538551 | 0.712 | 345.3 Da LogP -1.93 TPSA 197.6 | ✓ Ro5 | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…
|
| ZINC31475423 | 0.703 | 434.3 Da LogP -2.99 TPSA 238.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…
|
| ZINC105469665 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…
|
| ZINC13527614 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…
|
| ZINC219330894 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…
|
| ZINC3873852 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…
|
| ZINC3873853 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…
|
| ZINC3873854 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…
|
| ZINC3873855 | 0.694 | 425.2 Da LogP -1.64 TPSA 223.4 | 2 viol. | ✓ Clean |
Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…
|
| ZINC5615251 | 0.677 | 375.3 Da LogP -0.55 TPSA 164.1 | 1 viol. | ✓ Clean |
COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…
|
| ZINC5615253 | 0.677 | 375.3 Da LogP -0.55 TPSA 164.1 | 1 viol. | ✓ Clean |
COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…
|
| ZINC5615258 | 0.677 | 375.3 Da LogP -0.55 TPSA 164.1 | 1 viol. | ✓ Clean |
COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…
|
| ZINC5615263 | 0.677 | 375.3 Da LogP -0.55 TPSA 164.1 | 1 viol. | ✓ Clean |
COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…
|
| ZINC31516918 | 0.672 | 446.4 Da LogP -1.33 TPSA 218.2 | 1 viol. | ✓ Clean |
CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…
|
| ZINC1582675 | 0.667 | 403.3 Da LogP 0.23 TPSA 164.1 | 1 viol. | ✓ Clean |
CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…
|
| ZINC5486730 | 0.667 | 403.3 Da LogP 0.23 TPSA 164.1 | 1 viol. | ✓ Clean |
CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…
|
| ZINC5486734 | 0.667 | 403.3 Da LogP 0.23 TPSA 164.1 | 1 viol. | ✓ Clean |
CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…
|
| ZINC5486740 | 0.667 | 403.3 Da LogP 0.23 TPSA 164.1 | 1 viol. | ✓ Clean |
CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…
|
PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.