Protein profile

PA5524

short-chain dehydrogenase

Genome: NC_002516.2

Gene: PA5524 Structure source: AlphaFold UniProt Q9HT49

Export view

Amino acids 260

Annotations 4

Features 23

PDB binders 4

Druggability 0.363

Overview

Basic information about this protein and its source genome.

Accession: PA5524
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5524
Status: annotated
Amino acids: 260
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 (%): 48.276
Human E-value: 3.38e-09
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 0.363

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
10	201	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.
21	251	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
9	253	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
9	253	InterPro	IPR036291	NAD(P)-binding domain superfamily
5	254	FunFam	G3DSA:3.40.50.720:FF:000173	3-oxoacyl-[acyl-carrier protein] reductase
145	153	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
145	153	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
166	185	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
166	185	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
86	97	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
86	97	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
8	252	PANTHER	PTHR42879	3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE
86	97	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
139	155	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
139	155	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
187	204	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
187	204	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
166	185	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
11	28	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
11	28	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
2	257	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.

Loading 3D structure...

Legend High Medium Low

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 PA5524	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				0.363

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
AAE	6ZZQ	A0A1E3M3N6	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=O)O`
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`
QT8	6ZZS	A0A1E3M3N6	116.1 Da LogP 0.44 TPSA 54.4	✓ Ro5	✓ Clean	`CCC(=O)CC(=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
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…`
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)…`
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`
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`
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`
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`
ZINC6092199	0.667	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	Alert	`O=c1cc(-c2ccc(O)c(O)c2)oc2cc(O)ccc12`
ZINC1561069	0.659	300.3 Da LogP 3.12 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc([C@H]2CC(=O)c3c(O)cc(OC)cc3O2)cc1`
ZINC2030112	0.659	300.3 Da LogP 3.12 TPSA 65.0	✓ Ro5	✓ Clean	`COc1ccc([C@@H]2CC(=O)c3c(O)cc(OC)cc3O2)cc1`
ZINC5004393	0.649	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	✓ Clean	`O=c1cc(-c2c(O)cc(O)cc2O)oc2cc(O)cc(O)c12`
ZINC14761164	0.643	300.3 Da LogP 2.59 TPSA 111.1	✓ Ro5	Alert	`Cc1c(O)cc2oc(-c3ccc(O)c(O)c3)cc(=O)c2c1O`
ZINC14756811	0.641	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1cc(-c2ccc(O)cc2O)oc2cc(O)cc(O)c12`
ZINC14756882	0.641	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1cc(-c2c(O)cccc2O)oc2cc(O)cc(O)c12`
ZINC30730397	0.634	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	Alert	`O=C1C[C@@H](c2ccc(O)cc2)Oc2cc(O)c(O)cc21`
ZINC30730402	0.634	272.3 Da LogP 2.51 TPSA 87.0	✓ Ro5	Alert	`O=C1C[C@H](c2ccc(O)cc2)Oc2cc(O)c(O)cc21`
ZINC14819291	0.633	340.4 Da LogP 4.02 TPSA 87.0	✓ Ro5	✓ Clean	`CC(C)=CCc1cc([C@@H]2CC(=O)c3c(O)cc(O)cc3O2)ccc1O`
ZINC14819293	0.633	340.4 Da LogP 4.02 TPSA 87.0	✓ Ro5	✓ Clean	`CC(C)=CCc1cc([C@H]2CC(=O)c3c(O)cc(O)cc3O2)ccc1O`
ZINC1106016	0.630	356.3 Da LogP 2.95 TPSA 99.1	✓ Ro5	✓ Clean	`CC(=O)Oc1ccc([C@H]2CC(=O)c3c(O)cc(OC(C)=O)cc3O2…`
ZINC14728437	0.630	302.3 Da LogP 2.52 TPSA 96.2	✓ Ro5	✓ Clean	`COc1c(O)cc2c(c1O)C(=O)C[C@H](c1ccc(O)cc1)O2`
ZINC14728438	0.630	302.3 Da LogP 2.52 TPSA 96.2	✓ Ro5	✓ Clean	`COc1c(O)cc2c(c1O)C(=O)C[C@@H](c1ccc(O)cc1)O2`

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.