Protein profile

PA2142

short-chain dehydrogenase

Genome: NC_002516.2

Gene: PA2142 Structure source: AlphaFold UniProt Q9I1X3

Export view

Amino acids 286

Annotations 2

Features 28

PDB binders 11

Druggability 0.276

Overview

Basic information about this protein and its source genome.

Accession: PA2142
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2142
Status: annotated
Amino acids: 286
Structure source: AlphaFold

GO:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. 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 (%): 46.667
Human E-value: 4.39e-08
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 0.276

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:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
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.

28 records

Show feature table

Start	End	DB	Term	Name
191	210	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
191	210	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
119	130	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
119	130	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
171	179	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
171	179	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
44	61	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
44	61	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
119	130	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
165	181	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
165	181	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
191	210	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
246	266	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
246	266	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
212	229	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
212	229	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	31	MobiDBLite	mobidb-lite	consensus disorder prediction
17	281	PANTHER	PTHR48107	NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED
2	284	Gene3D	G3DSA:3.40.50.720	-
43	228	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.
52	281	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
17	285	CDD	cd05355	SDR_c1
1	20	MobiDBLite	mobidb-lite	consensus disorder prediction
178	206	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
178	206	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
41	284	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
41	284	InterPro	IPR036291	NAD(P)-binding domain superfamily
28	285	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase

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 PA2142	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
4				0.276

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
A6O	6IHH	C0IR58	314.4 Da LogP 3.93 TPSA 46.5	✓ Ro5	✓ Clean	`CC[C@]1([C@H](CCC1=O)O)C/C=C/2\CCCc3c2ccc(c3)OC`
BUO	5OJG	G5EGA6	86.1 Da LogP 0.16 TPSA 34.1	✓ Ro5	Alert	`CC(=O)C(=O)C`
CAC	3I3O	A0A6L8PL20	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
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`
ISN	5OJI	G5EGA6	147.1 Da LogP 0.82 TPSA 46.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)C(=O)N2`
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`
NAE	3I3O	A0A6L8PL20	719.5 Da LogP -3.52 TPSA 338.2	3 viol.	✓ Clean	`CC(=O)Cc1cc[n+](cc1C(=O)N)[C@H]2[C@@H]([C@@H]([…`
QSO	4FJ2	O93874	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1ccc(cc1)C2=COc3cc(cc(c3C2=O)O)O`
TAM	4BMN	C0IR58	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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)…`
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`
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`
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`
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…`
ZINC4803379	1.000	238.3 Da LogP 3.44 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccccc1)OCc1ccccc1`
ZINC6116596	1.000	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)ccc12`
ZINC6018481	0.875	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(OC)cc(O)c3c2=O)cc1`
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)…`
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`
ZINC120273	0.806	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2cc(O)cc(O)c12`
ZINC2149675	0.806	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(-c2ccccc2)coc2cc(O)cc(O)c12`
ZINC57845	0.806	270.2 Da LogP 2.58 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2cccc(O)c2)oc2cc(O)ccc12`
ZINC2888441	0.794	272.7 Da LogP 4.10 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccccc1)OCc1ccc(Cl)cc1`
ZINC3103992	0.794	272.7 Da LogP 4.10 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(Cl)cc1)OCc1ccccc1`
ZINC3228605	0.794	256.3 Da LogP 3.58 TPSA 26.3	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc(F)cc1)OCc1ccccc1`
ZINC11865148	0.791	282.3 Da LogP 3.48 TPSA 59.7	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(C)c3c2=O)cc1`
ZINC14811807	0.791	298.3 Da LogP 3.18 TPSA 68.9	✓ Ro5	✓ Clean	`COc1ccc(-c2coc3cc(O)cc(OC)c3c2=O)cc1`
ZINC18847044	0.786	284.3 Da LogP 2.88 TPSA 79.9	✓ Ro5	✓ Clean	`COc1cc(O)c2c(=O)c(-c3ccc(O)cc3)coc2c1`
ZINC3869685	0.784	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	Alert	`O=c1c(O)c(-c2ccc(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC6092209	0.784	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	Alert	`O=c1c(-c2ccc(O)c(O)c2)coc2cc(O)cc(O)c12`
ZINC57648	0.778	254.2 Da LogP 2.87 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccccc2)oc2ccc(O)cc12`
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…`
ZINC103633384	0.759	296.3 Da LogP 3.03 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(/C=C\C(=O)OCc1ccccc1)OCc1ccccc1`
ZINC4411156	0.759	296.3 Da LogP 3.03 TPSA 52.6	✓ Ro5	✓ Clean	`O=C(/C=C/C(=O)OCc1ccccc1)OCc1ccccc1`
ZINC2556384	0.757	282.3 Da LogP 3.41 TPSA 72.8	✓ Ro5	✓ Clean	`COc1ccc2c(c1)oc1c3ccc(O)cc3oc(=O)c21`
ZINC1633891	0.750	268.3 Da LogP 3.45 TPSA 35.5	✓ Ro5	✓ Clean	`COc1ccc(/C=C/C(=O)OCc2ccccc2)cc1`
ZINC3874317	0.750	318.2 Da LogP 1.69 TPSA 151.6	1 viol.	Alert	`O=c1c(O)c(-c2cc(O)c(O)c(O)c2)oc2cc(O)cc(O)c12`
ZINC3881558	0.750	302.2 Da LogP 1.99 TPSA 131.4	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(O)cc2O)oc2cc(O)cc(O)c12`
ZINC584641356	0.750	338.2 Da LogP 3.60 TPSA 90.9	✓ Ro5	✓ Clean	`O=c1c(O)c(-c2ccc(C(F)(F)F)cc2)oc2cc(O)cc(O)c12`
ZINC6411540	0.750	300.3 Da LogP 2.59 TPSA 100.1	✓ Ro5	✓ Clean	`COc1ccc(-c2oc3cc(O)cc(O)c3c(=O)c2O)cc1`
ZINC6525249	0.750	286.2 Da LogP 2.28 TPSA 111.1	✓ Ro5	✓ Clean	`O=c1c(-c2ccc(O)cc2O)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.