Protein profile

PA4091

4-hydroxyphenylacetate 3-monooxygenase large subunit

Genome: NC_002516.2

Gene: hpaB PA4091 hpaA Structure source: AlphaFold UniProt Q9HWT7

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Amino acids 520

Annotations 7

Features 23

PDB binders 3

Druggability 0.799

Overview

Basic information about this protein and its source genome.

Accession: PA4091
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: hpaB PA4091 hpaA
Status: annotated
Amino acids: 520
Structure source: AlphaFold

1.14.14.9

GO:0052881 Catalysis of the reaction: (4-hydroxyphenyl)acetate + FADH(2) + O2 = 3,4-dihydroxyphenylacetate + FAD + H+ + H2O. 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:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. GO:0042803 Binding to an identical protein to form a homodimer. GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate. GO:0016712 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Selected Druggability evidence

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 0.799

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.14.14.9

Gene Ontology (GO)

GO:0052881 Catalysis of the reaction: (4-hydroxyphenyl)acetate + FADH(2) + O2 = 3,4-dihydroxyphenylacetate + FAD + H+ + H2O.
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:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0042803 Binding to an identical protein to form a homodimer.
GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate.
GO:0016712 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
284	500	FunFam	G3DSA:1.20.140.10:FF:000044	4-hydroxyphenylacetate 3-monooxygenase oxygenase component
2	520	NCBIfam	TIGR02310	4-hydroxyphenylacetate 3-monooxygenase, oxygenase component
2	520	InterPro	IPR012688	4-hydroxyphenylacetate 3-monooxygenase oxygenase component, gammaproteobacteria
1	518	PIRSF	PIRSF500125	4_HPA_large
1	518	InterPro	IPR024677	4-HPA 3-monooxygenase large component/Pyoverdin chromophore biosynthetic protein
13	151	FunFam	G3DSA:1.10.3140.10:FF:000001	4-hydroxyphenylacetate 3-monooxygenase oxygenase component
288	477	Pfam	PF03241	4-hydroxyphenylacetate 3-hydroxylase C terminal
288	477	InterPro	IPR024719	HpaB/PvcC/4-BUDH C-terminal
156	282	Gene3D	G3DSA:2.40.110.10	-
156	282	InterPro	IPR046373	Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
272	494	SUPERFAMILY	SSF47203	Acyl-CoA dehydrogenase C-terminal domain-like
272	494	InterPro	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal
152	282	FunFam	G3DSA:2.40.110.10:FF:000026	4-hydroxyphenylacetate 3-monooxygenase oxygenase component
11	501	PIRSF	PIRSF000331	HpaA_HpaB
11	501	InterPro	IPR004925	HpaB/PvcC/4-BUDH
6	514	PANTHER	PTHR36117	4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED
6	514	InterPro	IPR004925	HpaB/PvcC/4-BUDH
284	500	Gene3D	G3DSA:1.20.140.10	-
13	282	SUPERFAMILY	SSF56645	Acyl-CoA dehydrogenase NM domain-like
13	282	InterPro	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
14	155	Gene3D	G3DSA:1.10.3140.10	-
15	280	Pfam	PF11794	4-hydroxyphenylacetate 3-hydroxylase N terminal
15	280	InterPro	IPR024674	HpaB/PvcC/4-BUDH N-terminal

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA4091	AlphaFold	—	—	full sequence	—	Viewing

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
1				0.799
3				0.36

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.

53 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
4HP	2YYJ	Q5SJP8	152.1 Da LogP 1.02 TPSA 57.5	✓ Ro5	✓ Clean	`c1cc(ccc1CC(=O)O)O`
FDA	7E8P	Q53008	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
NPO	7E8P	Q53008	139.1 Da LogP 1.30 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(ccc1[N+](=O)[O-])O`

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
ZINC32222424	0.864	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(O)cc2)cc1`
ZINC1507107	0.857	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc(O)cc2)cc1`
ZINC100009138	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(/N=N\c2ccc(O)cc2)cc1`
ZINC100009140	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(/N=N/c2ccc(O)cc2)cc1`
ZINC13836765	0.750	247.3 Da LogP 3.45 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Sc2ccc(O)cc2)cc1`
ZINC189331	0.750	279.3 Da LogP 2.13 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)c2ccc(O)cc2)cc1`
ZINC1911545360	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC225426	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC254392989	0.750	243.2 Da LogP 3.72 TPSA 88.1	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N=Nc2ccc(O)cc2)cc1`
ZINC33246164	0.750	241.2 Da LogP 3.47 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC370769	0.750	231.2 Da LogP 3.09 TPSA 72.6	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Oc2ccc(O)cc2)cc1`
ZINC38237571	0.750	243.2 Da LogP 2.53 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(c1ccc(O)cc1)c1ccc([N+](=O)[O-])cc1`
ZINC8419013	0.750	230.2 Da LogP 3.04 TPSA 75.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Nc2ccc(O)cc2)cc1`
ZINC1682664	0.682	270.3 Da LogP 2.61 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(CC(=O)O)cc2)cc1`
ZINC391495	0.682	298.3 Da LogP 2.73 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(CCc2ccc(CC(=O)O)cc2)cc1`
ZINC21982756	0.667	299.3 Da LogP 2.63 TPSA 69.9	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N2CCN(c3ccc(O)cc3)CC2)cc1`
ZINC33835370	0.667	273.2 Da LogP 2.94 TPSA 104.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(O)cc1)Nc1ccc([N+](=O)[O-])cc1`
ZINC575442763	0.667	314.3 Da LogP 2.66 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(COCc2ccc(CC(=O)O)cc2)cc1`
ZINC33604885	0.630	202.2 Da LogP 2.17 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc2cc(O)ccc2c1`
ZINC895813	0.630	209.2 Da LogP 0.14 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)Cc1ccc(O)cc1`
ZINC156360	0.625	262.0 Da LogP 1.92 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(I)cc1`
ZINC167159	0.625	215.0 Da LogP 2.08 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Br)cc1`
ZINC1604377	0.619	320.3 Da LogP 4.84 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc(-c3ccc([N+](=O)[O-])cc…`
ZINC1648209	0.619	244.2 Da LogP 3.17 TPSA 86.3	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2ccc([N+](=O)[O-])cc2)cc1`
ZINC2173334	0.609	300.2 Da LogP 2.57 TPSA 120.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[…`
ZINC145787882	0.600	259.2 Da LogP 2.52 TPSA 89.7	✓ Ro5	✓ Clean	`O=C(Oc1ccc([N+](=O)[O-])cc1)c1ccc(O)cc1`
ZINC1699472	0.600	286.3 Da LogP 2.73 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Oc2ccc(CC(=O)O)cc2)cc1`
ZINC18036964	0.600	242.2 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/C=N/c2ccc(O)cc2)cc1`
ZINC18099346	0.600	242.2 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(/N=C/c2ccc(O)cc2)cc1`
ZINC225997	0.600	258.2 Da LogP 2.55 TPSA 92.5	✓ Ro5	✓ Clean	`O=C(Nc1ccc(O)cc1)c1ccc([N+](=O)[O-])cc1`
ZINC2318	0.600	212.2 Da LogP 2.98 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccccc2)cc1`
ZINC36019045	0.600	276.2 Da LogP 2.58 TPSA 126.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(O)c(-c2cc([N+](=O)[O-])ccc2O)…`
ZINC369682	0.600	294.3 Da LogP 2.10 TPSA 109.5	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(S(=O)(=O)Nc2ccc(O)cc2)cc1`
ZINC3750843	0.600	226.3 Da LogP 2.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(Cc2ccccc2)cc1`
ZINC39297153	0.600	228.2 Da LogP 2.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(Cc1ccc(O)cc1)c1ccc(O)cc1`
ZINC1688116	0.583	272.2 Da LogP 2.73 TPSA 103.3	✓ Ro5	✓ Clean	`O=C(c1ccc([N+](=O)[O-])cc1)c1ccc([N+](=O)[O-])c…`
ZINC5731136	0.581	278.3 Da LogP 2.44 TPSA 92.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc([S@](=O)Nc2ccc(O)cc2)cc1`
ZINC5731137	0.581	278.3 Da LogP 2.44 TPSA 92.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc([S@@](=O)Nc2ccc(O)cc2)cc1`
ZINC1256693	0.577	226.3 Da LogP 3.29 TPSA 37.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(CC(=O)O)cc2)cc1`
ZINC195766543	0.577	328.4 Da LogP 1.76 TPSA 74.6	✓ Ro5	✓ Clean	`C[Si](C)(c1ccc(CC(=O)O)cc1)c1ccc(CC(=O)O)cc1`
ZINC220053800	0.577	242.3 Da LogP 2.47 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2ccc(CO)cc2)cc1`
ZINC2539986	0.571	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2cccc(O)c2)cc1`
ZINC33427614	0.571	215.2 Da LogP 2.97 TPSA 63.4	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(-c2ccc(O)cc2)c1`
ZINC139174928	0.567	228.2 Da LogP 2.69 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(-c2cccc(O)c2)cc1`
ZINC1511626	0.565	249.0 Da LogP 2.20 TPSA 43.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(I)cc1`
ZINC1666827	0.565	202.0 Da LogP 2.36 TPSA 43.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(Br)cc1`
ZINC4616626	0.563	257.2 Da LogP 2.75 TPSA 87.8	✓ Ro5	Alert	`O=[N+]([O-])c1ccc(N/N=C/c2ccc(O)cc2)cc1`
ZINC7718004	0.563	269.3 Da LogP 3.20 TPSA 80.4	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc([N+](=O)[O-])cc1)c1ccc(O)cc1`
ZINC104058859	0.560	395.3 Da LogP 3.70 TPSA 149.7	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(C(O)(c2ccc([N+](=O)[O-])cc2)c…`
ZINC2584252	0.560	203.2 Da LogP 0.84 TPSA 97.5	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(S(=O)(=O)O)cc1`

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.