Protein profile

KP13_02174

2-octaprenyl-6-methoxyphenol hydroxylase

Genome: KpKP13

Gene: ubiH AHE42744.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GY55

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Amino acids 392

Annotations 7

Features 26

PDB binders 12

Druggability 0.954

Overview

Basic information about this protein and its source genome.

Accession: KP13_02174
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: ubiH AHE42744.1
Status: annotated
Amino acids: 392
Structure source: AlphaFold + ColabFold

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:0008681 Catalysis of the reaction: 2-methoxy-6-(all-trans-octaprenyl)phenol + H+ + NADPH + O2 = 2-methoxy-6-all-trans-octaprenyl-1,4-benzoquinol + H2O + NADP+. 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 28.117
Human E-value: 4.05e-33
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 76.02
DEG E-value: 0.0
Localization: Unknown
ColabFold pLDDT: 90.2

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 0.954

Structure A0A0H3GY55

Pocket Pocket 9

P2Rank 0.991

Structure A0A0H3GY55

Pocket Pocket 1

ColabFold model

FPocket 0.998 · Pocket 1

P2Rank 0.937 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 114 / 4744 genomes with a hit

Normalized 0.024

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

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:0008681 Catalysis of the reaction: 2-methoxy-6-(all-trans-octaprenyl)phenol + H+ + NADPH + O2 = 2-methoxy-6-all-trans-octaprenyl-1,4-benzoquinol + H2O + NADP+.
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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
293	309	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
278	293	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
2	24	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
154	169	PRINTS	PR00420	Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
1	18	Phobius	SIGNAL_PEPTIDE	Signal peptide region
3	388	NCBIfam	TIGR01984	2-octaprenyl-6-methoxyphenyl hydroxylase
3	388	InterPro	IPR011295	2-polyprenyl-6-methoxyphenol 4-hydroxylase
2	380	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	380	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
14	18	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
3	383	PANTHER	PTHR43876	UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL
1	213	FunFam	G3DSA:3.50.50.60:FF:000123	2-octaprenyl-6-methoxyphenyl hydroxylase
292	305	ProSitePatterns	PS01304	ubiH/COQ6 monooxygenase family signature.
292	305	InterPro	IPR018168	Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site
3	387	NCBIfam	TIGR01988	ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family
3	387	InterPro	IPR010971	Ubiquinone biosynthesis hydroxylase UbiH/COQ6
3	13	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
258	388	FunFam	G3DSA:3.50.50.60:FF:000021	Ubiquinone biosynthesis monooxygenase COQ6
2	336	Pfam	PF01494	FAD binding domain
2	336	InterPro	IPR002938	FAD-binding domain
19	392	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
253	391	Gene3D	G3DSA:3.50.50.60	-
253	391	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	203	Gene3D	G3DSA:3.50.50.60	-
1	203	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily

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...

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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_A0A0H3GY55	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02174	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
9				0.954

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	Score	Probability
1	23.9	0.893
2	23.31	0.888
3	1.74	0.031
4	1.53	0.022

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
1				0.998

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	Score	Probability
1	23.7	0.891
2	16.49	0.78
3	3.48	0.127
4	2.34	0.061

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.

63 records

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	6SW2	Q9HWJ1	179.2 Da LogP 0.93 TPSA 80.4	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)CC(=O)O)N`
APR	2PHH	P00438	559.3 Da LogP -3.28 TPSA 291.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BHA	1PBC	P00438	153.1 Da LogP 0.67 TPSA 83.5	✓ Ro5	✓ Clean	`c1cc(c(cc1N)O)C(=O)O`
CTC	5TUI	A0A059WYP6	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`C[C@]1(c2c(ccc(c2C(=O)C3=C([C@]4([C@@H](C[C@@H]…`
DHB	6JU1	P20586	154.1 Da LogP 0.80 TPSA 77.8	✓ Ro5	Alert	`c1cc(c(cc1C(=O)O)O)O`
DOB	1DOD	P20586	154.1 Da LogP 0.80 TPSA 77.8	✓ Ro5	✓ Clean	`c1cc(c(cc1O)O)C(=O)O`
FAS	1PDH	P00438	785.6 Da LogP -2.42 TPSA 362.9	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@H]([C@@…`
PAB	1IUS	P20586	137.1 Da LogP 0.97 TPSA 63.3	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)N`
PHB	1D7L	P20586	138.1 Da LogP 1.09 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1C(=O)O)O`
PSL	1YKJ	P20586	176.1 Da LogP -2.08 TPSA 123.6	✓ Ro5	✓ Clean	`[O-]S(=O)(=O)OS(=O)(=O)[O-]`
RFL	1D7L	P20586	814.6 Da LogP -2.67 TPSA 366.2	3 viol.	✓ Clean	`Cc1cc2c(cc1N(C)C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]…`
RFP	6BRD	F2R776	823.0 Da LogP 4.34 TPSA 220.1	3 viol.	Alert	`Cc1c(c2c3c4c1O[C@@](C4=O)(O\C=C\[C@@H]([C@H]([C…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL130259	P00438	7.23	244.2 Da LogP 2.67 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)c1ccc(O)cc1OCc1ccccc1`

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
ZINC14768423	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC19701767	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC19701769	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC22054932	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…`
ZINC34800280	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC35024403	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC43769566	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC44019569	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`
ZINC44830179	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC71789581	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC86860183	1.000	478.9 Da LogP 0.44 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`
ZINC1245666585	0.850	289.3 Da LogP 4.30 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(-c2ccc(-c3ccc(C(=O)O)cc3)cc2)cc1`
ZINC1746121	0.850	213.2 Da LogP 2.63 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(-c2ccc(C(=O)O)cc2)cc1`
ZINC22018837	0.850	241.2 Da LogP 2.20 TPSA 80.4	✓ Ro5	✓ Clean	`Nc1ccc(C(=O)c2ccc(C(=O)O)cc2)cc1`
ZINC389804	0.842	214.2 Da LogP 2.76 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(O)cc2)cc1`
ZINC11525121	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC18202167	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC20410403	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC21984166	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC239173596	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4059755	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4215819	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…`
ZINC43771554	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…`
ZINC4807269	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC575338663	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…`
ZINC84441937	0.762	444.4 Da LogP -0.21 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…`
ZINC100412109	0.739	241.3 Da LogP 3.38 TPSA 88.0	✓ Ro5	Alert	`Nc1ccc(/N=N\c2ccc(C(=O)O)cc2)cc1`
ZINC113407075	0.739	237.3 Da LogP 2.37 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(C#Cc2ccc(C(=O)O)cc2)cc1`
ZINC127654	0.739	229.2 Da LogP 2.76 TPSA 72.5	✓ Ro5	Alert	`Nc1ccc(Oc2ccc(C(=O)O)cc2)cc1`
ZINC1628139	0.739	239.3 Da LogP 3.14 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(/C=C/c2ccc(C(=O)O)cc2)cc1`
ZINC17285708	0.739	239.3 Da LogP 3.14 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1ccc(/C=C\c2ccc(C(=O)O)cc2)cc1`
ZINC17322332	0.739	241.3 Da LogP 3.38 TPSA 88.0	✓ Ro5	Alert	`Nc1ccc(N=Nc2ccc(C(=O)O)cc2)cc1`
ZINC1750451	0.739	227.3 Da LogP 2.56 TPSA 63.3	✓ Ro5	Alert	`Nc1ccc(Cc2ccc(C(=O)O)cc2)cc1`
ZINC4707411	0.739	241.3 Da LogP 3.38 TPSA 88.0	✓ Ro5	Alert	`Nc1ccc(/N=N/c2ccc(C(=O)O)cc2)cc1`
ZINC148781474	0.727	274.2 Da LogP 2.16 TPSA 115.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2ccc(C(=O)O)cc2O)c(O)c1`
ZINC33246180	0.727	242.2 Da LogP 3.51 TPSA 82.2	✓ Ro5	Alert	`O=C(O)c1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC3896282	0.727	242.2 Da LogP 3.51 TPSA 82.2	✓ Ro5	Alert	`O=C(O)c1ccc(/N=N/c2ccc(O)cc2)cc1`
ZINC392302	0.727	230.2 Da LogP 2.88 TPSA 66.8	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Oc2ccc(O)cc2)cc1`
ZINC13084338	0.722	242.3 Da LogP 3.27 TPSA 46.5	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)O)c(OCc2ccccc2)c1`
ZINC91297263	0.722	246.2 Da LogP 3.10 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)c1ccc(F)cc1OCc1ccccc1`
ZINC1675321	0.714	274.2 Da LogP 1.57 TPSA 115.1	✓ Ro5	Alert	`O=C(C(=O)c1ccc(O)c(O)c1)c1ccc(O)c(O)c1`
ZINC100302624	0.701	478.9 Da LogP 0.28 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(=O)C(C(N)=O)=C(O)[C@@]2(O)C(=O)C3…`
ZINC100302627	0.701	478.9 Da LogP 0.28 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(=O)C(C(N)=O)=C(O)[C@@]2(O)C(=O)C3…`
ZINC198557834	0.701	478.9 Da LogP 0.28 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(=O)C(C(N)=O)=C(O)[C@]2(O)C(=O)C3=…`
ZINC198557874	0.701	478.9 Da LogP 0.28 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(=O)C(C(N)=O)=C(O)[C@]2(O)C(=O)C3=…`
ZINC199209020	0.701	478.9 Da LogP 0.28 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(=O)C(C(N)=O)=C(O)[C@]2(O)C(=O)C3=…`
ZINC256411188	0.701	478.9 Da LogP 0.28 TPSA 181.6	1 viol.	✓ Clean	`CN(C)[C@@H]1C(=O)C(C(N)=O)=C(O)[C@]2(O)C(=O)C3=…`
ZINC2169206	0.697	228.2 Da LogP 2.96 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1OCc1ccccc1`
ZINC1587804	0.696	274.2 Da LogP 1.57 TPSA 115.1	✓ Ro5	Alert	`O=C(C(=O)c1ccc(O)cc1O)c1ccc(O)cc1O`
ZINC39103	0.696	246.2 Da LogP 1.74 TPSA 98.0	✓ Ro5	✓ Clean	`O=C(c1ccc(O)cc1O)c1ccc(O)cc1O`

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.