Protein profile

PA4389

3-ketoacyl-ACP reductase

Genome: NC_002516.2

Gene: speA PA4389 Structure source: AlphaFold UniProt Q9HW15

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Amino acids 252

Annotations 4

Features 23

PDB binders 3

Druggability 0.836

Overview

Basic information about this protein and its source genome.

Accession: PA4389
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: speA PA4389
Status: annotated
Amino acids: 252
Structure source: AlphaFold

1.3.1.58

GO:0018511 Catalysis of the reaction: cis-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+ = 2,3-dihydroxy-p-cumate + H+ + NADH. 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. GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 41.767
Human E-value: 9.96e-52
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 0.836

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1.3.1.58

Gene Ontology (GO)

GO:0018511 Catalysis of the reaction: cis-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+ = 2,3-dihydroxy-p-cumate + H+ + NADH.
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.
GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
6	193	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.
1	252	FunFam	G3DSA:3.40.50.720:FF:000173	3-oxoacyl-[acyl-carrier protein] reductase
4	250	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
4	250	InterPro	IPR036291	NAD(P)-binding domain superfamily
183	200	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
183	200	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
7	24	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
7	24	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
216	236	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
216	236	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
81	92	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
81	92	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
162	181	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
162	181	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
137	153	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
137	153	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	252	Gene3D	G3DSA:3.40.50.720	-
2	250	PANTHER	PTHR42760	SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER
81	92	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
143	151	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
143	151	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
162	181	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
15	250	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase

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 PA4389	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				0.836

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.

58 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
B3P	4NBV	B3R6T4	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`C(CNC(CO)(CO)CO)CNC(CO)(CO)CO`
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…`
P4C	3EZL	Q3JRS9	324.4 Da LogP -0.72 TPSA 92.7	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCC=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
KDH	Q8I2S7	6.50	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`c1c(cc(c(c1O)O)O)[C@@H]2[C@@H](Cc3c(cc(cc3O2)O)…`
LU2	Q965D6	6.10	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O`
CHEMBL129451	Q965D6	6.00	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
CHEMBL36327	Q965D6	6.00	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
NAR	Q965D6	—	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	✓ Clean	`c1cc(ccc1[C@@H]2CC(=O)c3c(cc(cc3O2)O)O)O`

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
ZINC156701	1.000	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	✓ Clean	`O=C1C[C@@H](c2ccc(O)cc2)Oc2cc(O)cc(O)c21`
ZINC1785	1.000	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	✓ Clean	`O=C1C[C@H](c2ccc(O)cc2)Oc2cc(O)cc(O)c21`
ZINC18185774	1.000	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC3870412	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC3870413	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC3870414	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC3870415	1.000	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC4521259	1.000	282.3 Da LogP -4.01 TPSA 145.4	1 viol.	✓ Clean	`OCC(CO)(CO)NCCCNC(CO)(CO)CO`
ZINC14436185	0.854	472.4 Da LogP 2.54 TPSA 186.4	2 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC3978503	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)…`
ZINC4534390	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)c(O)c…`
ZINC4544252	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c1…`
ZINC8681494	0.851	442.4 Da LogP 2.53 TPSA 177.1	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1ccc(O)c(O)c…`
ZINC14727965	0.848	426.4 Da LogP 2.82 TPSA 156.9	1 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1ccc(O)cc1)…`
ZINC4935	0.816	256.3 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`O=C1C[C@H](c2ccccc2)Oc2cc(O)cc(O)c21`
ZINC73693	0.816	256.3 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`O=C1C[C@@H](c2ccccc2)Oc2cc(O)cc(O)c21`
ZINC14728393	0.806	288.3 Da LogP 2.22 TPSA 107.2	✓ Ro5	✓ Clean	`O=C1C[C@@H](c2cc(O)cc(O)c2)Oc2cc(O)cc(O)c21`
ZINC58116	0.795	288.3 Da LogP 2.22 TPSA 107.2	✓ Ro5	Alert	`O=C1C[C@H](c2ccc(O)c(O)c2)Oc2cc(O)cc(O)c21`
ZINC58117	0.795	288.3 Da LogP 2.22 TPSA 107.2	✓ Ro5	Alert	`O=C1C[C@@H](c2ccc(O)c(O)c2)Oc2cc(O)cc(O)c21`
ZINC3871576	0.778	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(O)cc2)oc2cc(O)cc(O)c12`
ZINC4348965	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@H](c1ccc(O)cc1)CC2=O`
ZINC4348970	0.775	270.3 Da LogP 3.11 TPSA 66.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)O[C@@H](c1ccc(O)cc1)CC2=O`
ZINC2146973	0.762	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1ccc([C@@H]2CC(=O)c3c(O)cc(O)cc3O2)cc1`
ZINC895707	0.762	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1ccc([C@H]2CC(=O)c3c(O)cc(O)cc3O2)cc1`
ZINC21992193	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c…`
ZINC21992196	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@@H]1c1cc(O)c(O)c(…`
ZINC21992198	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(…`
ZINC21992201	0.760	458.4 Da LogP 2.23 TPSA 197.4	2 viol.	Alert	`O=C(O[C@H]1Cc2c(O)cc(O)cc2O[C@H]1c1cc(O)c(O)c(O…`
ZINC14813714	0.750	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	Alert	`COc1cc(O)c2c(=O)cc(-c3ccc(O)c(O)c3)oc2c1`
ZINC338283	0.738	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)c2c(c1)O[C@@H](c1ccc(O)cc1)CC2=O`
ZINC338284	0.738	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)c2c(c1)O[C@H](c1ccc(O)cc1)CC2=O`
ZINC13520048	0.730	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`O=c1cc(-c2cc(O)c(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC39317	0.730	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cccc(O)c12`
ZINC14642643	0.722	456.4 Da LogP 2.83 TPSA 166.1	1 viol.	Alert	`COc1cc(C(=O)O[C@@H]2Cc3c(O)cc(O)cc3O[C@@H]2c2cc…`
ZINC6536308	0.718	288.7 Da LogP 3.52 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(Cl)cc2)oc2cc(O)cc(O)c12`
ZINC14813748	0.714	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	Alert	`COc1cc(O)cc2oc(-c3ccc(O)c(O)c3)cc(=O)c12`
ZINC519621	0.714	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1cc(-c2cc(=O)c3c(O)cc(O)cc3o2)ccc1O`
ZINC5733652	0.714	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(=O)c3c(O)cc(O)cc3o2)cc1O`
ZINC3872070	0.711	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1cc(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC14728095	0.700	288.3 Da LogP 2.22 TPSA 107.2	✓ Ro5	✓ Clean	`O=C1C[C@H](c2c(O)cccc2O)Oc2cc(O)cc(O)c21`
ZINC6091723	0.700	288.3 Da LogP 2.22 TPSA 107.2	✓ Ro5	✓ Clean	`O=C1C[C@@H](c2c(O)cccc2O)Oc2cc(O)cc(O)c21`
ZINC14757037	0.698	366.3 Da LogP 1.76 TPSA 154.5	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(OS(=O)(=O)O)cc(O)c…`
ZINC5999024	0.698	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)cc2c1C(=O)C[C@H](c1ccc(O)cc1)O2`
ZINC5999025	0.698	286.3 Da LogP 2.81 TPSA 76.0	✓ Ro5	✓ Clean	`COc1cc(O)cc2c1C(=O)C[C@@H](c1ccc(O)cc1)O2`
ZINC39091	0.689	302.3 Da LogP 2.52 TPSA 96.2	✓ Ro5	✓ Clean	`COc1ccc([C@H]2CC(=O)c3c(O)cc(O)cc3O2)cc1O`
ZINC39092	0.689	302.3 Da LogP 2.52 TPSA 96.2	✓ Ro5	✓ Clean	`COc1ccc([C@@H]2CC(=O)c3c(O)cc(O)cc3O2)cc1O`
ZINC1730318	0.674	286.3 Da LogP 2.82 TPSA 87.0	✓ Ro5	✓ Clean	`Cc1c(O)cc2c(c1O)C(=O)C[C@H](c1ccc(O)cc1)O2`
ZINC5202283	0.674	286.3 Da LogP 2.82 TPSA 87.0	✓ Ro5	✓ Clean	`Cc1c(O)cc2c(c1O)C(=O)C[C@@H](c1ccc(O)cc1)O2`
ZINC6018693	0.674	314.3 Da LogP 2.89 TPSA 89.1	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(=O)c3c(O)cc(O)cc3o2)cc1OC`
ZINC3871358	0.667	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(-c2cc(=O)c3c(O)cc(O)cc3o2)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.