Protein profile

PA0182

3-ketoacyl-ACP reductase

Genome: NC_002516.2

Gene: PA0182 Structure source: AlphaFold UniProt Q9I6V0

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Amino acids 250

Annotations 1

Features 24

PDB binders 12

Druggability 0.879

Overview

Basic information about this protein and its source genome.

Accession: PA0182
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA0182
Status: annotated
Amino acids: 250
Structure source: AlphaFold

GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 43.617
Human E-value: 6.96e-07
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.879

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Gene Ontology (GO)

GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
132	148	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
132	148	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
159	178	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
159	178	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
180	197	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
180	197	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
212	232	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
212	232	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
87	98	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
87	98	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
12	29	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
12	29	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
5	248	PANTHER	PTHR42760	SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER
13	245	CDD	cd05233	SDR_c
10	249	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
10	249	InterPro	IPR036291	NAD(P)-binding domain superfamily
87	98	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
138	146	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
138	146	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
159	178	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
2	249	FunFam	G3DSA:3.40.50.720:FF:000290	SDR family oxidoreductase
19	249	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
11	190	SMART	SM00822	This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
2	249	Gene3D	G3DSA:3.40.50.720	-

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 PA0182	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				0.879
3				0.796

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
AOI	1NFQ	P9WGT1	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](C[C@@H]1CC[C@@H]3[C@@H]2CC[C@]4(…`
BEA	1YBV	Q12634	190.3 Da LogP 1.67 TPSA 31.4	✓ Ro5	✓ Clean	`Cc1cccc2c1n3cn[nH+]c3s2`
CAA	3VZS	P14697	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
CUE	3QWI	O93874	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`c1cc2c(cc1O)oc-3c2C(=O)Oc4c3ccc(c4)O`
GEN	4FJ1	O93874	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O`
HHF	4FJ0	O93874	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`c1ccc(cc1)C2=C(C(=O)c3ccc(cc3O2)O)O`
KMP	3QWH	O93874	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`c1cc(ccc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O`
NID	1DOH	Q12634	175.1 Da LogP 1.80 TPSA 60.2	✓ Ro5	✓ Clean	`c1cc2c(c(c1)[N+](=O)[O-])C=CC2=O`
PG0	5Z2L	P39333	120.1 Da LogP -0.36 TPSA 38.7	✓ Ro5	✓ Clean	`COCCOCCO`
PHH	1G0N	Q12634	271.9 Da LogP 3.97 TPSA 26.3	✓ Ro5	✓ Clean	`C1c2c(c(c(c(c2Cl)Cl)Cl)Cl)C(=O)O1`
PYQ	1G0O	Q12634	173.2 Da LogP 1.52 TPSA 20.3	✓ Ro5	✓ Clean	`c1cc2c3c(c1)CCN3C(=O)CC2`
QSO	4FJ2	O93874	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(cc1)C2=COc3cc(cc(c3C2=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL361197	O93874	6.16	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccccc1`

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
ZINC1219	1.000	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`O=c1oc2cc(O)ccc2c2oc3cc(O)ccc3c12`
ZINC12358883	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccccc1`
ZINC1580161	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1691401	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC1857742182	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(C=Cc1ccccc1)OCc1ccccc1`
ZINC18825330	1.000	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(O)cc2)coc2cc(O)cc(O)c12`
ZINC18847037	1.000	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(O)c3c2=O)cc1`
ZINC2012697	1.000	271.9 Da LogP 3.97 TPSA 26.3	✓ Ro5	✓ Clean	`O=C1OCc2c(Cl)c(Cl)c(Cl)c(Cl)c21`
ZINC253497590	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@H]1[C@H]2CC[C@@]2…`
ZINC253497948	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC253928529	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@]…`
ZINC34317654	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38145858	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC38145859	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@H](O)CC[C@@]…`
ZINC3849577	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@]…`
ZINC3849581	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@@H](O)CC[C@@…`
ZINC3849584	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@@H](O)CC[C@@]…`
ZINC3849784	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@H](O)CC[C@@]…`
ZINC3849785	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC3861550	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC3861661	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@H]4C[C@@H](O)CC[C@@]…`
ZINC3869419	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@@…`
ZINC3869768	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC3875364	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@@H]4C[C@H](O)CC[C@]3…`
ZINC4073949	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@@H](CC[C@H]4C[C@@H](O)CC[C@@…`
ZINC44076059	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4743888	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CC[C@@H]4C[C@@H](O)CC[C@]…`
ZINC4803379	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccccc1)OCc1ccccc1`
ZINC5210101	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6116596	1.000	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)ccc12`
ZINC7996759	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@@H](O)CC[C@@]…`
ZINC81132361	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@@…`
ZINC81132362	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@@…`
ZINC82230076	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@H](O)C[C@@H]1CC[C@@H]1[C@@H]2CC[C@@…`
ZINC9231975	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H](O)C[C@@H]1CC[C@H]1[C@H]2CC[C@@]…`
ZINC948	1.000	290.4 Da LogP 3.96 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@@H]4C[C@@H](O)CC[C@]…`
ZINC6018481	0.875	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(OC)cc(O)c3c2=O)cc1`
ZINC257345656	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC257345657	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC257345658	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@]43…`
ZINC257345659	0.854	304.5 Da LogP 4.35 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CC[C@H]4C[C@H](O)CC[C@@]4…`
ZINC14504998	0.844	254.3 Da LogP 3.15 TPSA 46.5	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(O)cc1)OCc1ccccc1`
ZINC39203780	0.844	268.2 Da LogP 3.10 TPSA 83.8	✓ Ro5	✓ Clean	`O=c1oc2cc(O)ccc2c2oc3ccc(O)cc3c12`
ZINC6093351	0.824	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2)oc2cc(O)ccc12`
ZINC304562	0.811	333.1 Da LogP 3.63 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(Br)cc2)coc2cc(O)cc(O)c12`
ZINC5731170	0.811	288.7 Da LogP 3.52 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(Cl)cc2)coc2cc(O)cc(O)c12`
ZINC5997152	0.811	272.2 Da LogP 3.01 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(F)cc2)coc2cc(O)cc(O)c12`

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.