Protein profile

PA5281

hydrolase

Genome: NC_002516.2

Gene: PA5281 Structure source: AlphaFold UniProt Q9HTS3

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Amino acids 232

Annotations 2

Features 20

PDB binders 5

Druggability 0.223

Overview

Basic information about this protein and its source genome.

Accession: PA5281
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5281
Status: annotated
Amino acids: 232
Structure source: AlphaFold

GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0009231 The chemical reactions and pathways resulting in the formation of riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 49.091
Human E-value: 1.15e-07
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 0.223

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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0009231 The chemical reactions and pathways resulting in the formation of riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
3	231	PANTHER	PTHR46470	N-ACYLNEURAMINATE-9-PHOSPHATASE
7	223	Gene3D	G3DSA:3.40.50.1000	-
7	223	InterPro	IPR023214	HAD superfamily
85	200	NCBIfam	TIGR01509	HAD-IA family hydrolase
85	200	InterPro	IPR006439	HAD hydrolase, subfamily IA
4	15	PRINTS	PR00413	Haloacid dehalogenase/epoxide hydrolase family signature
4	15	InterPro	IPR006439	HAD hydrolase, subfamily IA
190	203	PRINTS	PR00413	Haloacid dehalogenase/epoxide hydrolase family signature
190	203	InterPro	IPR006439	HAD hydrolase, subfamily IA
144	160	PRINTS	PR00413	Haloacid dehalogenase/epoxide hydrolase family signature
144	160	InterPro	IPR006439	HAD hydrolase, subfamily IA
18	104	Gene3D	G3DSA:1.20.120.1600	-
4	231	SFLD	SFLDG01129	C1.5: HAD, Beta-PGM, Phosphatase Like
5	229	SUPERFAMILY	SSF56784	HAD-like
5	229	InterPro	IPR036412	HAD-like superfamily
94	195	NCBIfam	TIGR01549	HAD-IA family hydrolase
94	195	InterPro	IPR006439	HAD hydrolase, subfamily IA
8	200	Pfam	PF13419	Haloacid dehalogenase-like hydrolase
8	200	InterPro	IPR041492	Haloacid dehalogenase-like hydrolase
4	231	SFLD	SFLDS00003	Haloacid Dehalogenase

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 PA5281	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				0.223

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.

55 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
AC0	6Q7N	O58216	120.2 Da LogP 1.89 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccccc1`
NHE	4YGR	B6YTD6	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
POP	2X4D	Q9H008	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
TBU	4YGQ	B6YTD6	74.1 Da LogP 0.78 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)(C)O`
VO4	4KNW	Q8TBE9	114.9 Da LogP -3.69 TPSA 86.2	✓ Ro5	✓ Clean	`[O-][V](=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
ZINC1710230	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC3200262	0.842	252.3 Da LogP 2.95 TPSA 51.2	✓ Ro5	Alert	`CC(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1`
ZINC36456728	0.800	224.3 Da LogP 3.12 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C(=O)c2ccccc2)cc1`
ZINC2004372	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3593496	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1039926	0.625	220.3 Da LogP 3.29 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C#Cc2ccccc2)cc1`
ZINC143028	0.625	228.3 Da LogP 4.04 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Sc2ccccc2)cc1`
ZINC1440490	0.625	222.3 Da LogP 4.06 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(/C=C/c2ccccc2)cc1`
ZINC14686440	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC14981993	0.625	224.3 Da LogP 3.12 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1cccc(C(=O)c2ccccc2)c1`
ZINC1562037	0.625	210.3 Da LogP 3.48 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Cc2ccccc2)cc1`
ZINC1675948	0.625	226.3 Da LogP 3.33 TPSA 41.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NNc2ccccc2)cc1`
ZINC1845686	0.625	224.3 Da LogP 3.67 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(CCc2ccccc2)cc1`
ZINC21999250	0.625	211.3 Da LogP 3.63 TPSA 29.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Nc2ccccc2)cc1`
ZINC261810	0.625	212.2 Da LogP 3.68 TPSA 26.3	✓ Ro5	✓ Clean	`CC(=O)c1ccc(Oc2ccccc2)cc1`
ZINC4798948	0.625	224.3 Da LogP 4.30 TPSA 41.8	✓ Ro5	Alert	`CC(=O)c1ccc(/N=N/c2ccccc2)cc1`
ZINC50452	0.615	240.3 Da LogP 3.11 TPSA 43.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(OC(=O)c2ccccc2)cc1`
ZINC586797	0.615	239.3 Da LogP 3.14 TPSA 46.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NC(=O)c2ccccc2)cc1`
ZINC1672966	0.611	210.2 Da LogP 2.75 TPSA 34.1	✓ Ro5	Alert	`O=C(C(=O)c1ccccc1)c1ccccc1`
ZINC1401590	0.600	244.3 Da LogP 3.06 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([S@](=O)c2ccccc2)cc1`
ZINC143035	0.600	260.3 Da LogP 2.72 TPSA 51.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc(S(=O)(=O)c2ccccc2)cc1`
ZINC34354396	0.600	224.3 Da LogP 4.04 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([C@@H](C)c2ccccc2)cc1`
ZINC34354398	0.600	224.3 Da LogP 4.04 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([C@H](C)c2ccccc2)cc1`
ZINC4073660	0.600	244.3 Da LogP 3.06 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc([S@@](=O)c2ccccc2)cc1`
ZINC56557	0.600	238.3 Da LogP 3.76 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(-c2ccc(C(C)=O)cc2)cc1`
ZINC336592	0.583	224.3 Da LogP 3.12 TPSA 34.1	✓ Ro5	✓ Clean	`CC(=O)c1ccccc1C(=O)c1ccccc1`
ZINC1577122	0.579	208.3 Da LogP 4.64 TPSA 0.0	✓ Ro5	✓ Clean	`C/C(=C(/C)c1ccccc1)c1ccccc1`
ZINC1590838	0.579	342.4 Da LogP 3.82 TPSA 68.3	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccccc2)cc1)c1ccccc1`
ZINC16133932	0.579	474.5 Da LogP 4.88 TPSA 102.4	✓ Ro5	Alert	`O=C(C(=O)c1ccc(C(=O)C(=O)c2ccc(C(=O)C(=O)c3cccc…`
ZINC3123872	0.579	208.3 Da LogP 4.64 TPSA 0.0	✓ Ro5	✓ Clean	`C/C(=C(\C)c1ccccc1)c1ccccc1`
ZINC117551598	0.577	253.3 Da LogP 3.57 TPSA 37.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N(C(C)=O)c2ccccc2)cc1`
ZINC13398039	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1556064	0.577	252.4 Da LogP 4.45 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(CCCCc2ccccc2)cc1`
ZINC1621063	0.577	268.3 Da LogP 2.82 TPSA 71.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C(=O)c2ccccc2C(=O)O)cc1`
ZINC1720928	0.577	238.3 Da LogP 4.06 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1ccc(CCCc2ccccc2)cc1`
ZINC2039629	0.577	222.3 Da LogP 4.06 TPSA 17.1	✓ Ro5	✓ Clean	`CC(=O)c1cccc(/C=C/c2ccccc2)c1`
ZINC2528012	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC47679	0.577	254.3 Da LogP 3.53 TPSA 58.2	✓ Ro5	✓ Clean	`CC(=O)c1ccc(NC(=O)Nc2ccccc2)cc1`
ZINC1604259	0.571	346.3 Da LogP 4.99 TPSA 51.2	✓ Ro5	✓ Clean	`O=C(c1ccccc1)P(C(=O)c1ccccc1)C(=O)c1ccccc1`
ZINC5613445	0.571	240.3 Da LogP 2.06 TPSA 38.0	✓ Ro5	✓ Clean	`CC(=O)c1cc[n+](CC(=O)c2ccccc2)cc1`
ZINC1606240	0.565	238.3 Da LogP 3.59 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C(=O)O)=C(c1ccccc1)c1ccccc1`
ZINC2559799	0.565	240.3 Da LogP 3.25 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(-c2ccc(C(=O)O)cc2)cc1`
ZINC146315135	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC19367005	0.560	224.4 Da LogP 2.83 TPSA 24.1	✓ Ro5	✓ Clean	`C1CCC(NCCNC2CCCCC2)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.