Protein profile

PA3277

short-chain dehydrogenase

Genome: NC_002516.2

Gene: PA3277 Structure source: AlphaFold UniProt Q9HYW4

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Amino acids 270

Annotations 2

Features 22

PDB binders 7

Druggability 0.893

Overview

Basic information about this protein and its source genome.

Accession: PA3277
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3277
Status: annotated
Amino acids: 270
Structure source: AlphaFold

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. GO:0008202 The chemical reactions and pathways involving steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 43.564
Human E-value: 5.36e-18
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 0.893

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: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.
GO:0008202 The chemical reactions and pathways involving steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
3	176	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.
5	258	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
5	258	InterPro	IPR036291	NAD(P)-binding domain superfamily
130	138	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
130	138	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
150	169	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
150	169	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
78	89	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
78	89	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
5	190	Pfam	PF00106	short chain dehydrogenase
5	190	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
124	140	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
124	140	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
171	188	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
171	188	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
78	89	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
150	169	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
4	21	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
4	21	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
3	268	Gene3D	G3DSA:3.40.50.720	-
7	221	CDD	cd05233	SDR_c
4	239	PANTHER	PTHR43391	RETINOL DEHYDROGENASE-RELATED

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 PA3277	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				0.893

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.

57 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
1PS	4URE	Q5P8S7	201.2 Da LogP -0.09 TPSA 61.1	✓ Ro5	✓ Clean	`c1cc[n+](cc1)CCCS(=O)(=O)[O-]`
AAE	6ZZQ	A0A1E3M3N6	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=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`
GGE	4YAI	C0SUJ9	320.3 Da LogP 1.88 TPSA 88.4	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@H](c2ccc(c(c2)OC)O)O`
ISZ	1XR3	P16544	135.1 Da LogP 1.25 TPSA 66.2	✓ Ro5	Alert	`[H]/N=N/C(=O)c1ccncc1`
MLH	6T65	V5VHN7	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c2cc(c(cc2n(c1CN(C)C)c3ccccc3)Br)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
ZINC1233995	1.000	417.3 Da LogP 4.34 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC16697966	1.000	320.3 Da LogP 1.88 TPSA 88.4	✓ Ro5	✓ Clean	`COc1cc([C@H](O)[C@H](CO)Oc2ccccc2OC)ccc1O`
ZINC16697968	1.000	320.3 Da LogP 1.88 TPSA 88.4	✓ Ro5	✓ Clean	`COc1cc([C@H](O)[C@@H](CO)Oc2ccccc2OC)ccc1O`
ZINC16697970	1.000	320.3 Da LogP 1.88 TPSA 88.4	✓ Ro5	✓ Clean	`COc1cc([C@@H](O)[C@H](CO)Oc2ccccc2OC)ccc1O`
ZINC2528037	1.000	320.3 Da LogP 1.88 TPSA 88.4	✓ Ro5	✓ Clean	`COc1cc([C@@H](O)[C@@H](CO)Oc2ccccc2OC)ccc1O`
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`
ZINC8453886	0.849	431.3 Da LogP 4.65 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccc(C)cc2)c2cc(Br)c(O)c…`
ZINC519737	0.816	334.4 Da LogP 2.19 TPSA 77.4	✓ Ro5	✓ Clean	`COc1ccc([C@@H](O)[C@H](CO)Oc2ccccc2OC)cc1OC`
ZINC519738	0.816	334.4 Da LogP 2.19 TPSA 77.4	✓ Ro5	✓ Clean	`COc1ccc([C@@H](O)[C@@H](CO)Oc2ccccc2OC)cc1OC`
ZINC519739	0.816	334.4 Da LogP 2.19 TPSA 77.4	✓ Ro5	✓ Clean	`COc1ccc([C@H](O)[C@H](CO)Oc2ccccc2OC)cc1OC`
ZINC519740	0.816	334.4 Da LogP 2.19 TPSA 77.4	✓ Ro5	✓ Clean	`COc1ccc([C@H](O)[C@@H](CO)Oc2ccccc2OC)cc1OC`
ZINC5222178	0.800	431.3 Da LogP 4.64 TPSA 43.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(OC)cc12`
ZINC34114040	0.750	350.4 Da LogP 1.89 TPSA 97.6	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@H](O)c1cc(OC)c(O)c(OC)c1`
ZINC95639160	0.750	350.4 Da LogP 1.89 TPSA 97.6	✓ Ro5	✓ Clean	`COc1ccccc1O[C@@H](CO)[C@H](O)c1cc(OC)c(O)c(OC)c1`
ZINC95639161	0.750	350.4 Da LogP 1.89 TPSA 97.6	✓ Ro5	✓ Clean	`COc1ccccc1O[C@@H](CO)[C@@H](O)c1cc(OC)c(O)c(OC)…`
ZINC95639162	0.750	350.4 Da LogP 1.89 TPSA 97.6	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@@H](O)c1cc(OC)c(O)c(OC)c1`
ZINC704414	0.736	374.2 Da LogP 4.58 TPSA 51.5	✓ Ro5	✓ Clean	`CCOC(=O)c1c(C)n(-c2ccccc2)c2cc(Br)c(O)cc12`
ZINC4095655	0.735	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)cc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC1421880	0.727	338.4 Da LogP 3.57 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2ccc(O)cc12`
ZINC196731442	0.725	290.3 Da LogP 1.87 TPSA 79.2	✓ Ro5	✓ Clean	`COc1ccccc1O[C@@H](CO)[C@H](O)c1ccc(O)cc1`
ZINC196731458	0.725	290.3 Da LogP 1.87 TPSA 79.2	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@H](O)c1ccc(O)cc1`
ZINC196731468	0.725	290.3 Da LogP 1.87 TPSA 79.2	✓ Ro5	✓ Clean	`COc1ccccc1O[C@@H](CO)[C@@H](O)c1ccc(O)cc1`
ZINC196731476	0.725	290.3 Da LogP 1.87 TPSA 79.2	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@@H](O)c1ccc(O)cc1`
ZINC6041173	0.712	443.3 Da LogP 4.87 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN2CCCC2)n(-c2ccccc2)c2cc(Br)c(O)cc…`
ZINC185093	0.707	304.3 Da LogP 2.91 TPSA 68.2	✓ Ro5	✓ Clean	`COc1cc([C@@H](O)[C@H](C)Oc2ccccc2OC)ccc1O`
ZINC185098	0.707	304.3 Da LogP 2.91 TPSA 68.2	✓ Ro5	✓ Clean	`COc1cc([C@@H](O)[C@@H](C)Oc2ccccc2OC)ccc1O`
ZINC185102	0.707	304.3 Da LogP 2.91 TPSA 68.2	✓ Ro5	✓ Clean	`COc1cc([C@H](O)[C@H](C)Oc2ccccc2OC)ccc1O`
ZINC185108	0.707	304.3 Da LogP 2.91 TPSA 68.2	✓ Ro5	✓ Clean	`COc1cc([C@H](O)[C@@H](C)Oc2ccccc2OC)ccc1O`
ZINC755533	0.704	355.2 Da LogP 2.88 TPSA 54.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN(C)C)n(C)c2cc(Br)c(O)cc12`
ZINC91691836	0.700	292.3 Da LogP 1.28 TPSA 110.4	✓ Ro5	Alert	`OC[C@H](Oc1ccccc1O)[C@H](O)c1ccc(O)c(O)c1`
ZINC91691837	0.700	292.3 Da LogP 1.28 TPSA 110.4	✓ Ro5	Alert	`OC[C@@H](Oc1ccccc1O)[C@H](O)c1ccc(O)c(O)c1`
ZINC91691838	0.700	292.3 Da LogP 1.28 TPSA 110.4	✓ Ro5	Alert	`OC[C@H](Oc1ccccc1O)[C@@H](O)c1ccc(O)c(O)c1`
ZINC91691839	0.700	292.3 Da LogP 1.28 TPSA 110.4	✓ Ro5	Alert	`OC[C@@H](Oc1ccccc1O)[C@@H](O)c1ccc(O)c(O)c1`
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`
ZINC12413720	0.695	474.4 Da LogP 4.40 TPSA 57.9	✓ Ro5	Alert	`CCOC(=O)c1c(CN(C)C)n(-c2ccccc2)c2cc(Br)c(O)c(CN…`
ZINC208014413	0.694	488.4 Da LogP 4.71 TPSA 66.7	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CNCCN(CC)CC)n(-c2ccccc2)c2cc(Br)c(O…`
ZINC115187826	0.692	274.3 Da LogP 2.17 TPSA 58.9	✓ Ro5	✓ Clean	`COc1ccccc1O[C@@H](CO)[C@@H](O)c1ccccc1`
ZINC115187828	0.692	274.3 Da LogP 2.17 TPSA 58.9	✓ Ro5	✓ Clean	`COc1ccccc1O[C@@H](CO)[C@H](O)c1ccccc1`
ZINC34399708	0.692	274.3 Da LogP 2.17 TPSA 58.9	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@H](O)c1ccccc1`
ZINC39127554	0.692	274.3 Da LogP 2.17 TPSA 58.9	✓ Ro5	✓ Clean	`COc1ccccc1O[C@H](CO)[C@@H](O)c1ccccc1`
ZINC19818217	0.689	472.4 Da LogP 4.02 TPSA 57.9	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN2CCN(C)CC2)n(-c2ccccc2)c2cc(Br)c(…`
ZINC3861630	0.688	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cccc(O)c1C2=O`
ZINC216621813	0.683	304.3 Da LogP 2.18 TPSA 68.2	✓ Ro5	✓ Clean	`COc1ccc([C@H](O)[C@@H](CO)Oc2ccccc2OC)cc1`
ZINC216621861	0.683	304.3 Da LogP 2.18 TPSA 68.2	✓ Ro5	✓ Clean	`COc1ccc([C@@H](O)[C@@H](CO)Oc2ccccc2OC)cc1`
ZINC216621909	0.683	304.3 Da LogP 2.18 TPSA 68.2	✓ Ro5	✓ Clean	`COc1ccc([C@H](O)[C@H](CO)Oc2ccccc2OC)cc1`
ZINC216621956	0.683	304.3 Da LogP 2.18 TPSA 68.2	✓ Ro5	✓ Clean	`COc1ccc([C@@H](O)[C@H](CO)Oc2ccccc2OC)cc1`
ZINC19790628	0.677	459.3 Da LogP 4.11 TPSA 63.9	✓ Ro5	✓ Clean	`CCOC(=O)c1c(CN2CCOCC2)n(-c2ccccc2)c2cc(Br)c(O)c…`
ZINC203535351	0.667	440.4 Da LogP 0.28 TPSA 158.3	1 viol.	✓ Clean	`COc1cc([C@H](O)[C@H](CO)Oc2c(OC)cc([C@H](O)[C@H…`
ZINC247919332	0.667	440.4 Da LogP 0.28 TPSA 158.3	1 viol.	✓ Clean	`COc1cc([C@H](O)[C@H](CO)Oc2c(OC)cc([C@H](O)[C@@…`
ZINC247919337	0.667	440.4 Da LogP 0.28 TPSA 158.3	1 viol.	✓ Clean	`COc1cc([C@H](O)[C@H](CO)Oc2c(OC)cc([C@@H](O)[C@…`

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.