Overview
Basic information about this protein and its source genome.
- Accession
- KP13_04320
- Gene
- AHE45554.1 dinG
- Status
- annotated
- Amino acids
- 718
- 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)
- N
- DEG identity (%)
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 89.58
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)
14- GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
- GO:0003676 Binding to a nucleic acid.
- GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
- GO:0016818 Catalysis of the hydrolysis of any acid anhydride which contains phosphorus.
- GO:0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
- 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:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0043139 Unwinding a DNA helix in the 5' to 3' direction, 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:0033677 Unwinding of a DNA/RNA duplex, i.e. a double helix in which a strand of DNA pairs with a complementary strand of RNA, driven by ATP hydrolysis.
- GO:0046872 Binding to a metal ion.
- GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
- GO:0009432 An error-prone process for repairing damaged microbial DNA.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 531 | 688 | Pfam | PF13307 | Helicase C-terminal domain |
| 531 | 688 | InterPro | IPR006555 | ATP-dependent helicase, C-terminal |
| 17 | 294 | ProSiteProfiles | PS51193 | Superfamilies 1 and 2 helicase ATP-binding type-2 domain profile. |
| 17 | 294 | InterPro | IPR014013 | Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type |
| 26 | 277 | Gene3D | G3DSA:3.40.50.300 | - |
| 26 | 277 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 27 | 689 | PANTHER | PTHR11472 | DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER |
| 27 | 689 | InterPro | IPR045028 | Helicase superfamily 1/2, DinG/Rad3-like |
| 503 | 687 | FunFam | G3DSA:3.40.50.300:FF:000685 | ATP-dependent DNA helicase DinG |
| 27 | 287 | FunFam | G3DSA:3.40.50.300:FF:000700 | ATP-dependent DNA helicase DinG |
| 197 | 264 | Pfam | PF06733 | DEAD_2 |
| 197 | 264 | InterPro | IPR010614 | RAD3-like helicase, DEAD |
| 544 | 676 | SMART | SM00491 | Cxpdneu3 |
| 544 | 676 | InterPro | IPR006555 | ATP-dependent helicase, C-terminal |
| 34 | 695 | Hamap | MF_02205 | ATP-dependent DNA helicase DinG [dinG]. |
| 34 | 695 | InterPro | IPR039000 | ATP-dependent DNA helicase DinG |
| 504 | 687 | Gene3D | G3DSA:3.40.50.300 | - |
| 504 | 687 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 23 | 307 | SMART | SM00487 | ultradead3 |
| 23 | 307 | InterPro | IPR014001 | Helicase superfamily 1/2, ATP-binding domain |
| 31 | 94 | Pfam | PF00270 | DEAD/DEAH box helicase |
| 31 | 94 | InterPro | IPR011545 | DEAD/DEAH box helicase domain |
| 46 | 670 | SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases |
| 46 | 670 | InterPro | IPR027417 | P-loop containing nucleoside triphosphate hydrolase |
| 18 | 294 | SMART | SM00488 | deadxpd |
| 18 | 294 | InterPro | IPR006554 | Helicase-like, DEXD box c2 type |
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_A0A0H3GUG0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_04320
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
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 |
|---|---|---|---|---|---|---|---|
| 28 | 0.659 |
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 | 12.81 | 0.663 | ||||||
| 2 | 7.67 | 0.405 | ||||||
| 3 | 4.31 | 0.178 | ||||||
| 4 | 4.12 | 0.166 | ||||||
| 5 | 3.76 | 0.145 |
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 |
|---|---|---|---|---|---|---|---|
| 11 | 0.597 |
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 | 14.65 | 0.729 | ||||||
| 2 | 8.77 | 0.469 | ||||||
| 3 | 6.31 | 0.316 | ||||||
| 4 | 4.11 | 0.166 | ||||||
| 5 | 3.72 | 0.142 |
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| BEF | P27296 | 66.0 Da LogP 0.88 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
[Be-](F)(F)F
|
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).
No virtual-screening candidates for this protein.
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.