Protein profile

KP13_02175

Protein visC

Genome: KpKP13

Gene: visC AHE42745.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GSY0
Amino acids 400
Annotations 8
Features 19
PDB binders 1
Druggability 0.908

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 model

Selected 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.

FPocket 0.908
Structure A0A0H3GSY0
Pocket Pocket 27
P2Rank 0.944
Structure A0A0H3GSY0
Pocket Pocket 1
ColabFold model
FPocket 0.295 · Pocket 27
P2Rank 0.962 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 122 / 4744 genomes with a hit
Normalized 0.026

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

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.

19 records
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.

3D visualization script Full viewer

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Structural evidence

0 + 2

Experimental 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

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.

27 records

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.

Show only:
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

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.