Overview
Basic information about this protein and its source genome.
- Accession
- KP13_02175
- Gene
- visC AHE42745.1
- Status
- annotated
- Amino acids
- 400
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 37.017
- Human E-value
- 2.9600000000000004e-21
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 54.408
- DEG E-value
- 8.979999999999999e-150
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 88.42
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.
Gene Ontology (GO)
8- GO:0016709 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.
- GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
- GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
- GO:0016705 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor.
- GO:0006744 The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0110142 A protein complex composed of enzymes and accessory factors of the ubiquinone (CoQ) biosynthesis pathway. In E. coli, the complex is composed of seven proteins: UbiE, F, G, H, I, J and K. In eukaryotes, the complex is located on the matrix face of the inner mitochondrial membrane and includes COQ3, COQ4, COQ5, COQ6, COQ7, COQ9.
- GO:0019168 Catalysis of the reaction: a 2-(all-trans-polyprenyl)phenol + NADPH + O2 + H+ = a 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 396 | PANTHER | PTHR43876 | UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL |
| 295 | 308 | ProSitePatterns | PS01304 | ubiH/COQ6 monooxygenase family signature. |
| 295 | 308 | InterPro | IPR018168 | Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site |
| 5 | 391 | NCBIfam | TIGR01988 | ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family |
| 5 | 391 | InterPro | IPR010971 | Ubiquinone biosynthesis hydroxylase UbiH/COQ6 |
| 281 | 296 | PRINTS | PR00420 | Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature |
| 5 | 27 | PRINTS | PR00420 | Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature |
| 156 | 171 | PRINTS | PR00420 | Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature |
| 296 | 312 | PRINTS | PR00420 | Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature |
| 256 | 400 | FunFam | G3DSA:3.50.50.60:FF:000062 | FAD-dependent 2-octaprenylphenol hydroxylase |
| 259 | 400 | Gene3D | G3DSA:3.50.50.60 | - |
| 259 | 400 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 1 | 256 | Gene3D | G3DSA:3.50.50.60 | - |
| 1 | 256 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 1 | 254 | FunFam | G3DSA:3.50.50.60:FF:000048 | 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase |
| 4 | 385 | SUPERFAMILY | SSF51905 | FAD/NAD(P)-binding domain |
| 4 | 385 | InterPro | IPR036188 | FAD/NAD(P)-binding domain superfamily |
| 4 | 345 | Pfam | PF01494 | FAD binding domain |
| 4 | 345 | InterPro | IPR002938 | FAD-binding domain |
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_A0A0H3GSY0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_02175
|
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 |
|---|---|---|---|---|---|---|---|
| 27 | 0.908 | ||||||
| 6 | 0.264 |
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 | 27.37 | 0.92 | ||||||
| 2 | 13.22 | 0.678 | ||||||
| 3 | 7.02 | 0.363 | ||||||
| 4 | 4.2 | 0.171 | ||||||
| 5 | 2.37 | 0.062 |
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 |
|---|---|---|---|---|---|---|---|
| 27 | 0.295 |
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 | 28.93 | 0.928 | ||||||
| 2 | 20.83 | 0.863 | ||||||
| 3 | 6.54 | 0.331 | ||||||
| 4 | 5.99 | 0.295 | ||||||
| 5 | 2.27 | 0.056 |
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 |
|---|---|---|---|---|---|---|
| 61M | Q9HWJ1 | 179.2 Da LogP 0.93 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
c1ccc(c(c1)C(=O)CC(=O)O)N
|
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 |
|---|---|---|---|---|---|
| ZINC13356583 | 0.667 | 207.2 Da LogP 1.71 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)CCCC(=O)O
|
| ZINC343704 | 0.643 | 208.2 Da LogP 1.04 TPSA 91.7 | ✓ Ro5 | ✓ Clean |
O=C(O)CC(=O)c1ccccc1C(=O)O
|
| ZINC1059491 | 0.633 | 211.3 Da LogP 2.69 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)Cc1ccccc1
|
| ZINC1612530 | 0.594 | 225.3 Da LogP 3.08 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)CCc1ccccc1
|
| ZINC4235287 | 0.594 | 213.3 Da LogP 1.44 TPSA 47.0 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)C[n+]1ccccc1
|
| ZINC1715395 | 0.581 | 214.2 Da LogP 2.50 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
O=C(O)CC(=O)c1cccc2ccccc12
|
| ZINC895186 | 0.576 | 208.2 Da LogP 0.25 TPSA 106.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)C[C@H](N)C(=O)O
|
| ZINC901103 | 0.576 | 208.2 Da LogP 0.25 TPSA 106.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)C[C@@H](N)C(=O)O
|
| ZINC216654421 | 0.563 | 214.2 Da LogP -0.26 TPSA 103.2 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)CS(N)(=O)=O
|
| ZINC34352328 | 0.559 | 207.2 Da LogP 1.40 TPSA 69.4 | ✓ Ro5 | ✓ Clean |
COC(=O)CCC(=O)c1ccccc1N
|
| ZINC36047644 | 0.559 | 208.2 Da LogP 0.47 TPSA 92.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)NCCC(=O)O
|
| ZINC5162233 | 0.556 | 212.3 Da LogP 2.08 TPSA 69.1 | ✓ Ro5 | Alert |
Nc1ccccc1C(=O)c1ccccc1N
|
| ZINC2228897 | 0.548 | 298.3 Da LogP 1.01 TPSA 110.2 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)NCCNC(=O)c1ccccc1N
|
| ZINC1616708 | 0.543 | 269.3 Da LogP 2.78 TPSA 80.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)CCc1ccccc1C(=O)O
|
| ZINC150129 | 0.531 | 212.3 Da LogP 2.52 TPSA 55.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)Nc1ccccc1
|
| ZINC3886415 | 0.529 | 226.3 Da LogP 2.20 TPSA 55.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)NCc1ccccc1
|
| ZINC85434286 | 0.529 | 245.7 Da LogP 3.35 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)Cc1ccccc1Cl
|
| ZINC32314 | 0.516 | 241.2 Da LogP 2.20 TPSA 80.4 | ✓ Ro5 | Alert |
Nc1ccccc1C(=O)c1ccccc1C(=O)O
|
| ZINC40564460 | 0.516 | 216.0 Da LogP 1.73 TPSA 63.3 | ✓ Ro5 | ✓ Clean |
Nc1cccc(C(=O)O)c1Br
|
| ZINC3083759 | 0.514 | 255.3 Da LogP 2.31 TPSA 69.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)OCC(=O)c1ccccc1
|
| ZINC128305 | 0.500 | 240.3 Da LogP 2.24 TPSA 55.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)NCCc1ccccc1
|
| ZINC1875257564 | 0.500 | 241.3 Da LogP 1.78 TPSA 81.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1CNC(=O)c1ccccc1N
|
| ZINC2169730 | 0.500 | 227.3 Da LogP 2.63 TPSA 52.3 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)OCc1ccccc1
|
| ZINC22577051 | 0.500 | 384.5 Da LogP 0.19 TPSA 134.3 | 1 viol. | ✓ Clean |
Nc1ccccc1C(=O)NCCNCCNCCNC(=O)c1ccccc1N
|
| ZINC4343010 | 0.500 | 217.3 Da LogP 2.76 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)Cc1cccs1
|
| ZINC70286739 | 0.500 | 242.3 Da LogP 2.13 TPSA 64.4 | ✓ Ro5 | ✓ Clean |
Nc1ccccc1C(=O)NOCc1ccccc1
|
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.