Protein profile

PA1933

hydroxylase large subunit

Genome: NC_002516.2

Gene: PA1933 Structure source: AlphaFold UniProt Q9I2H1

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Amino acids 734

Annotations 2

Features 19

PDB binders 9

Druggability 0.511

Overview

Basic information about this protein and its source genome.

Accession: PA1933
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1933
Status: annotated
Amino acids: 734
Structure source: AlphaFold

GO:0005506 Binding to an iron (Fe) ion. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 24.183
Human E-value: 6.77e-29
Gut microbiome off-target: hit
Essential (DEG): N
Localization: CytoplasmicMembrane

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 0.511

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Gene Ontology (GO)

GO:0005506 Binding to an iron (Fe) ion.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records

Show feature table

Start	End	DB	Term	Name
22	135	Pfam	PF01315	Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
22	135	InterPro	IPR000674	Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
22	136	SMART	SM01008	Ald_Xan_dh_C_2
22	136	InterPro	IPR000674	Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
3	136	Gene3D	G3DSA:3.90.1170.50	Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
9	721	PANTHER	PTHR11908	XANTHINE DEHYDROGENASE
9	721	InterPro	IPR016208	Aldehyde oxidase/xanthine dehydrogenase
406	675	Pfam	PF20256	Molybdopterin cofactor-binding domain
406	675	InterPro	IPR046867	Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain
184	276	Gene3D	G3DSA:3.30.365.10	Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain
153	382	Pfam	PF02738	Molybdopterin cofactor-binding domain
153	382	InterPro	IPR008274	Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain
446	590	Gene3D	G3DSA:3.30.365.10	Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain
159	382	Gene3D	G3DSA:3.30.365.10	Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain
7	147	SUPERFAMILY	SSF54665	CO dehydrogenase molybdoprotein N-domain-like
7	147	InterPro	IPR036856	Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily
137	733	SUPERFAMILY	SSF56003	Molybdenum cofactor-binding domain
137	733	InterPro	IPR037165	Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily
591	727	Gene3D	G3DSA:3.30.365.10	Aldehyde oxidase/xanthine dehydrogenase, molybdopterin 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.

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Structural evidence

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA1933	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				0.511
2				0.285

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.

59 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
2MO	1DGJ	Q9REC4	127.9 Da LogP -0.24 TPSA 34.1	✓ Ro5	✓ Clean	`O=[Mo]=O`
3PL	4US9	Q46509	134.2 Da LogP 1.82 TPSA 17.1	✓ Ro5	✓ Clean	`c1ccc(cc1)CCC=O`
CSD	5G5H	P77489	153.2 Da LogP -1.38 TPSA 100.6	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)N)[S@@](=O)O`
FES	1RM6	O33819	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HBX	4US8	Q46509	106.1 Da LogP 1.50 TPSA 17.1	✓ Ro5	✓ Clean	`c1ccc(cc1)C=O`
HCI	4USA	Q46509	150.2 Da LogP 1.70 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)CCC(=O)O`
MCN	5G5G	P77489	696.5 Da LogP -1.29 TPSA 319.9	3 viol.	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
MOS	5G5G	P77489	161.0 Da LogP 0.14 TPSA 34.1	✓ Ro5	✓ Clean	`O=[Mo](=O)S`
PEO	4C7Y	Q46509	34.0 Da LogP 0.02 TPSA 40.5	✓ Ro5	✓ Clean	`OO`

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
ZINC406914	0.800	222.2 Da LogP 1.72 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(CCC(=O)O)cc1`
ZINC2038070571	0.778	208.3 Da LogP 3.67 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1ccc(C=Cc2ccccc2)cc1`
ZINC2539416	0.778	208.3 Da LogP 3.67 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1ccc(/C=C/c2ccccc2)cc1`
ZINC83325301	0.778	208.3 Da LogP 3.67 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1ccc(/C=C\c2ccccc2)cc1`
ZINC9998612	0.750	226.3 Da LogP 3.37 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(-c2ccccc2)cc1`
ZINC2163727	0.739	222.2 Da LogP 1.72 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(CCC(=O)O)c1`
ZINC88278178	0.739	210.3 Da LogP 3.49 TPSA 17.1	✓ Ro5	✓ Clean	`O=CCCc1ccc(-c2ccccc2)cc1`
ZINC1673354	0.727	238.3 Da LogP 3.82 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)CCc1ccccc1`
ZINC1693912	0.727	266.3 Da LogP 3.39 TPSA 34.1	✓ Ro5	Alert	`O=C(CCc1ccccc1)C(=O)CCc1ccccc1`
ZINC247409588	0.692	220.3 Da LogP 2.44 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCc1ccccc1`
ZINC38256625	0.684	258.3 Da LogP 4.83 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1`
ZINC72232709	0.682	224.2 Da LogP -2.44 TPSA 143.7	✓ Ro5	✓ Clean	`N[C@@H](CS(=O)C[C@H](N)C(=O)O)C(=O)O`
ZINC1558609	0.680	248.4 Da LogP 4.43 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCc1ccccc1`
ZINC2510086	0.680	262.4 Da LogP 4.82 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCc1ccccc1`
ZINC2575483	0.680	206.3 Da LogP 3.26 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCc1ccccc1`
ZINC2575484	0.680	220.3 Da LogP 3.65 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCc1ccccc1`
ZINC2575485	0.680	234.3 Da LogP 4.04 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCc1ccccc1`
ZINC11962728	0.667	242.3 Da LogP 3.50 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(Oc2ccccc2)cc1`
ZINC49820418	0.667	226.3 Da LogP 3.37 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(-c2ccccc2)c1`
ZINC163985	0.655	256.3 Da LogP 3.28 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(OCc2ccccc2)cc1`
ZINC85210604	0.643	240.3 Da LogP 3.40 TPSA 26.3	✓ Ro5	✓ Clean	`O=CCCc1ccc(OCc2ccccc2)cc1`
ZINC1089845	0.640	210.3 Da LogP 3.50 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)c1ccccc1`
ZINC15780483	0.640	224.3 Da LogP 3.43 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)Cc1ccccc1`
ZINC1663872	0.640	276.1 Da LogP 2.31 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(I)cc1`
ZINC2574309	0.640	229.1 Da LogP 2.47 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(Br)cc1`
ZINC19814467	0.633	283.3 Da LogP 2.89 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(NC(=O)Cc2ccccc2)cc1`
ZINC14620416	0.615	314.3 Da LogP 3.51 TPSA 83.8	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(Oc2ccc(CCC(=O)O)cc2)cc1`
ZINC3298861	0.615	326.4 Da LogP 3.34 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)OCCOC(=O)CCc1ccccc1`
ZINC536954149	0.613	284.3 Da LogP 3.06 TPSA 63.6	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(C(=O)OCc2ccccc2)cc1`
ZINC1675915	0.607	200.2 Da LogP 2.86 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc2ccccc2c1`
ZINC2574308	0.607	229.1 Da LogP 2.47 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(Br)c1`
ZINC2580671	0.607	276.1 Da LogP 2.31 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(I)c1`
ZINC4672223	0.607	207.2 Da LogP 0.82 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)CCc1ccccc1`
ZINC1727327	0.600	208.2 Da LogP 1.33 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1ccccc1CC(=O)O`
ZINC19809009	0.600	242.3 Da LogP 3.50 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(Oc2ccccc2)c1`
ZINC2565818	0.600	304.4 Da LogP 4.99 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(/C=C/C=C/C=C/c2ccccc2)cc1`
ZINC31416155	0.600	304.4 Da LogP 4.99 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(/C=C/C=C/C=C\c2ccccc2)cc1`
ZINC393260	0.600	322.4 Da LogP 4.03 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1c2ccccc2c(CCC(=O)O)c2ccccc12`
ZINC1258844	0.593	240.3 Da LogP 3.68 TPSA 37.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(CCC(=O)O)cc2)cc1`
ZINC16698049	0.593	206.3 Da LogP 2.90 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)Cc1ccc(CCC(=O)O)cc1`
ZINC339196	0.593	242.3 Da LogP 3.08 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(-c2ccc(O)cc2)cc1`
ZINC409787	0.593	326.4 Da LogP 3.70 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCc1ccc(Cc2ccc(CCC(=O)O)cc2)cc1`
ZINC4206065	0.593	206.3 Da LogP 3.00 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(CCC(=O)O)cc1`
ZINC6096123	0.593	202.2 Da LogP 2.75 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)C(F)(F)F`
ZINC6281402	0.593	324.4 Da LogP 2.48 TPSA 58.2	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)NCCNC(=O)CCc1ccccc1`
ZINC1583082	0.591	273.3 Da LogP 4.97 TPSA 20.3	✓ Ro5	✓ Clean	`O=Cc1ccc(N(c2ccccc2)c2ccccc2)cc1`
ZINC2003724	0.591	214.3 Da LogP 3.65 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1ccc(Sc2ccccc2)cc1`
ZINC2159115	0.591	206.2 Da LogP 2.90 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1ccc(C#Cc2ccccc2)cc1`
ZINC335166	0.591	301.3 Da LogP 4.78 TPSA 37.4	✓ Ro5	✓ Clean	`O=Cc1ccc(N(c2ccccc2)c2ccc(C=O)cc2)cc1`
ZINC22113357	0.586	230.3 Da LogP 2.89 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(Cc2ccccc2)o1`

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.