Protein profile

PA3957

short-chain dehydrogenase

Genome: NC_002516.2

Gene: PA3957 Structure source: AlphaFold UniProt Q9HX59

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Amino acids 278

Annotations 2

Features 29

PDB binders 8

Druggability 0.808

Overview

Basic information about this protein and its source genome.

Accession: PA3957
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3957
Status: annotated
Amino acids: 278
Structure source: AlphaFold

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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 (%): 45.714
Human E-value: 1.46e-14
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 0.808

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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
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.

29 records

Show feature table

Start	End	DB	Term	Name
2	271	Gene3D	G3DSA:3.40.50.720	-
31	278	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
11	268	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
11	268	InterPro	IPR036291	NAD(P)-binding domain superfamily
149	177	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
149	177	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
14	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.
14	202	Pfam	PF00106	short chain dehydrogenase
14	202	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
6	274	PANTHER	PTHR44196	DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B
7	249	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
26	30	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
90	101	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
90	101	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
162	181	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
162	181	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
142	150	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
142	150	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	30	Phobius	SIGNAL_PEPTIDE	Signal peptide region
15	25	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
90	101	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
15	32	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
15	32	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
162	181	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
183	200	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
183	200	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
136	152	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
136	152	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
1	14	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.

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

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA3957	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				0.808
3				0.603

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.

56 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
3HR	3VDR	D0VWQ0	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@H](CC(=O)O)O`
AAE	6ZZQ	A0A1E3M3N6	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=O)O`
DXX	3W8D	D0VWQ0	118.1 Da LogP -0.21 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C(=O)O)C(=O)O`
EMO	2RH4	P16544	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc2c(c(c1)O)C(=O)c3c(cc(cc3O)O)C2=O`
HBR	6XEW	H9XP47	88.1 Da LogP -0.04 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](C(=O)C)O`
ISZ	1XR3	P16544	135.1 Da LogP 1.25 TPSA 66.2	✓ Ro5	Alert	`[H]/N=N/C(=O)c1ccncc1`
MLA	3W8F	D0VWQ0	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=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).

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
ZINC3824868	1.000	270.2 Da LogP 1.89 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC4095655	0.735	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)cc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC3978794	0.697	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)c2c(c1)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC3861630	0.688	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cccc(O)c1C2=O`
ZINC14760847	0.667	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC5277130	0.656	238.2 Da LogP 2.48 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1ccccc1C2=O`
ZINC4098655	0.629	304.7 Da LogP 2.54 TPSA 94.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(Cl)c(O)c1C2=O`
ZINC5461939	0.618	286.2 Da LogP 1.59 TPSA 115.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1O)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14814143	0.595	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1c(O)ccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13481200	0.594	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)cc(O)cc21`
ZINC3977762	0.588	300.2 Da LogP 1.28 TPSA 132.1	✓ Ro5	Alert	`O=C(O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC5812872	0.588	286.2 Da LogP 1.07 TPSA 115.1	✓ Ro5	Alert	`O=C1c2cc(O)cc(O)c2C(=O)c2c(O)cc(CO)cc21`
ZINC6070245	0.588	256.3 Da LogP 2.25 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1cc(O)c2c(c1)Cc1cc(O)cc(O)c1C2=O`
ZINC14760863	0.579	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1c(O)c(C)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC6070262	0.579	314.2 Da LogP 1.59 TPSA 132.1	✓ Ro5	Alert	`Cc1cc2c(c(O)c1C(=O)O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC14819806	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC14819808	0.568	314.3 Da LogP 1.50 TPSA 115.1	✓ Ro5	Alert	`C[C@H](O)Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O)c1C2=O`
ZINC31163880	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc…`
ZINC31163884	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163888	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(…`
ZINC31163892	0.568	330.3 Da LogP 0.99 TPSA 135.3	✓ Ro5	Alert	`C[C@H](O)[C@H](O)c1cc(O)c2c(c1)C(=O)c1cc(O)cc(O…`
ZINC13334425	0.564	268.3 Da LogP 2.48 TPSA 63.6	✓ Ro5	Alert	`COc1cccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13546016	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC13546018	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@@H](C)CC(=O)O`
ZINC257400894	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC257400895	0.560	276.3 Da LogP 0.49 TPSA 110.1	✓ Ro5	✓ Clean	`C[C@H](O)CC(=O)O[C@@H](C)CC(=O)O[C@H](C)CC(=O)O`
ZINC14760819	0.553	300.3 Da LogP 1.90 TPSA 104.1	✓ Ro5	Alert	`COc1cc(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC5412537	0.553	316.3 Da LogP 1.60 TPSA 124.3	✓ Ro5	Alert	`COc1c(O)c(O)c2c(c1O)C(=O)c1cc(C)cc(O)c1C2=O`
ZINC20111521	0.550	327.3 Da LogP 1.95 TPSA 98.1	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)c(CN(C)C)c(O)c1C2=O`
ZINC77257242	0.538	316.3 Da LogP 1.43 TPSA 124.3	✓ Ro5	Alert	`COCc1c(O)cc2c(c1O)C(=O)c1c(O)cc(O)cc1C2=O`
ZINC1637808	0.528	267.1 Da LogP 2.36 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)C=C(Br)C2=O`
ZINC14811261	0.512	300.3 Da LogP 1.37 TPSA 104.1	✓ Ro5	Alert	`COc1cc(CO)cc2c1C(=O)c1c(O)cc(O)cc1C2=O`
ZINC137596932	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@H]3O[C@@H](CO…`
ZINC2053539354	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@H]3O[C@H](CO)…`
ZINC2080144947	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@H]3O[C@H](CO)…`
ZINC2080147051	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O…`
ZINC238733159	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@H]2O[C@@H](CO)[C@H](O)[C@@H](O)[C@@H]…`
ZINC238774329	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@H](CO…`
ZINC253593197	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@@H](C…`
ZINC253598174	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@@H]2O[C@@H](CO)[C@H](O)[C@@H](O)[C@@H…`
ZINC33832450	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O[C@@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2…`
ZINC4098672	0.510	432.4 Da LogP -0.64 TPSA 174.0	1 viol.	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O)cc(O[C@@H]3O[C@H](CO…`
ZINC14814264	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@@H]3O[C@H](C)[C@@H…`
ZINC14814268	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@H]3O[C@H](C)[C@@H]…`
ZINC2332918206	0.500	388.8 Da LogP 2.98 TPSA 107.0	✓ Ro5	Alert	`CC(=O)Oc1cc2c(c(OC(C)=O)c1Cl)C(=O)c1c(O)cc(C)cc…`
ZINC253477263	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@@H]3O[C@H](C)[C@H]…`
ZINC31425373	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@H]3O[C@@H](C)[C@H]…`
ZINC4098673	0.500	416.4 Da LogP 0.39 TPSA 153.8	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cc(O[C@@H]3O[C@@H](C)[C@H…`

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.