Protein profile

PA5521

short-chain dehydrogenase

Genome: NC_002516.2

Gene: PA5521 Structure source: AlphaFold UniProt Q9HT52

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Amino acids 252

Annotations 3

Features 31

PDB binders 6

Druggability 0.622

Overview

Basic information about this protein and its source genome.

Accession: PA5521
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5521
Status: annotated
Amino acids: 252
Structure source: AlphaFold

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. 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 (%): 39.806
Human E-value: 7.31e-11
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 0.622

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

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.
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.

31 records

Show feature table

Start	End	DB	Term	Name
21	252	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
16	20	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
10	249	Pfam	PF13561	Enoyl-(Acyl carrier protein) reductase
5	15	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
5	250	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
5	250	InterPro	IPR036291	NAD(P)-binding domain superfamily
4	186	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.
212	232	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
212	232	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
147	166	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
147	166	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
75	86	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
75	86	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
121	137	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
121	137	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
5	22	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
5	22	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
168	185	PRINTS	PR00081	Glucose/ribitol dehydrogenase family signature
168	185	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
2	249	PANTHER	PTHR43639	OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870)
6	245	CDD	cd05233	SDR_c
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	252	FunFam	G3DSA:3.40.50.720:FF:000084	Short-chain dehydrogenase reductase
127	135	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
127	135	InterPro	IPR002347	Short-chain dehydrogenase/reductase SDR
147	166	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
75	86	PRINTS	PR00080	Short-chain dehydrogenase/reductase (SDR) superfamily signature
134	162	ProSitePatterns	PS00061	Short-chain dehydrogenases/reductases family signature.
134	162	InterPro	IPR020904	Short-chain dehydrogenase/reductase, conserved site
1	20	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	251	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.

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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 PA5521	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				0.622
4				0.612

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
3HL	2ZTL	Q5KST5	104.1 Da LogP -0.16 TPSA 57.5	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)O)O`
5XC	5FFF	A0A1A9TAK5	150.1 Da LogP 1.23 TPSA 35.5	✓ Ro5	✓ Clean	`c1cc2c(cc1C=O)OCO2`
AEF	5FF9	A0A1A9TAK5	137.2 Da LogP 0.89 TPSA 46.2	✓ Ro5	✓ Clean	`c1cc(ccc1CCN)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`

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)…`

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`
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)…`
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…`
ZINC13681005	0.750	229.3 Da LogP 2.69 TPSA 55.5	✓ Ro5	✓ Clean	`NCCc1ccc(Oc2ccc(O)cc2)cc1`
ZINC4095655	0.735	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1cc(O)cc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC8729752	0.724	226.2 Da LogP 2.89 TPSA 35.5	✓ Ro5	✓ Clean	`O=Cc1ccc(-c2ccc3c(c2)OCO3)cc1`
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…`
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`
ZINC17877731	0.690	340.4 Da LogP 1.34 TPSA 72.5	✓ Ro5	✓ Clean	`O=Cc1ccc2c(c1)OCCOCCOCCOCCOCCO2`
ZINC4566282	0.690	416.4 Da LogP 2.57 TPSA 89.5	✓ Ro5	✓ Clean	`O=Cc1ccc2c(c1)OCCOCCOc1ccc(C=O)cc1OCCOCCO2`
ZINC4737459	0.690	416.4 Da LogP 2.57 TPSA 89.5	✓ Ro5	✓ Clean	`O=Cc1ccc2c(c1)OCCOCCOc1cc(C=O)ccc1OCCOCCO2`
ZINC4975920	0.690	296.3 Da LogP 1.32 TPSA 63.2	✓ Ro5	✓ Clean	`O=Cc1ccc2c(c1)OCCOCCOCCOCCO2`
ZINC74735	0.690	252.3 Da LogP 1.30 TPSA 54.0	✓ Ro5	✓ Clean	`O=Cc1ccc2c(c1)OCCOCCOCCO2`
ZINC3861630	0.688	254.2 Da LogP 2.18 TPSA 74.6	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1cccc(O)c1C2=O`
ZINC1562031	0.684	214.3 Da LogP 2.88 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(CCc2ccc(O)cc2)cc1`
ZINC34925604	0.682	213.3 Da LogP 2.76 TPSA 46.2	✓ Ro5	Alert	`Nc1ccc(CCc2ccc(O)cc2)cc1`
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`
ZINC33427554	0.656	226.2 Da LogP 2.89 TPSA 35.5	✓ Ro5	✓ Clean	`O=Cc1cccc(-c2ccc3c(c2)OCO3)c1`
ZINC5277130	0.656	238.2 Da LogP 2.48 TPSA 54.4	✓ Ro5	Alert	`Cc1cc(O)c2c(c1)C(=O)c1ccccc1C2=O`
ZINC2390999	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)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`
ZINC47845246	0.625	227.3 Da LogP 3.15 TPSA 46.2	✓ Ro5	Alert	`Nc1ccc(CCCc2ccc(O)cc2)cc1`
ZINC3870336	0.622	306.3 Da LogP 1.25 TPSA 130.6	1 viol.	Alert	`Oc1cc(O)c2c(c1)O[C@H](c1cc(O)c(O)c(O)c1)[C@H](O…`
ZINC3870337	0.622	306.3 Da LogP 1.25 TPSA 130.6	1 viol.	Alert	`Oc1cc(O)c2c(c1)O[C@@H](c1cc(O)c(O)c(O)c1)[C@H](…`
ZINC3870338	0.622	306.3 Da LogP 1.25 TPSA 130.6	1 viol.	Alert	`Oc1cc(O)c2c(c1)O[C@H](c1cc(O)c(O)c(O)c1)[C@@H](…`
ZINC3870339	0.622	306.3 Da LogP 1.25 TPSA 130.6	1 viol.	Alert	`Oc1cc(O)c2c(c1)O[C@@H](c1cc(O)c(O)c(O)c1)[C@@H]…`
ZINC1602323	0.621	296.3 Da LogP 2.60 TPSA 61.6	✓ Ro5	✓ Clean	`C(=N/N=C/c1ccc2c(c1)OCO2)\c1ccc2c(c1)OCO2`
ZINC17163879	0.621	296.3 Da LogP 2.60 TPSA 61.6	✓ Ro5	✓ Clean	`C(=N\N=C/c1ccc2c(c1)OCO2)\c1ccc2c(c1)OCO2`
ZINC8652404	0.621	296.3 Da LogP 2.60 TPSA 61.6	✓ Ro5	✓ Clean	`C(=N\N=C\c1ccc2c(c1)OCO2)\c1ccc2c(c1)OCO2`
ZINC1556073	0.619	228.3 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(CCCc2ccc(O)cc2)cc1`
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`
ZINC1405419	0.609	232.7 Da LogP 3.83 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1ccc(CCc2ccc(Cl)cc2)cc1`
ZINC14814143	0.595	284.3 Da LogP 2.19 TPSA 83.8	✓ Ro5	Alert	`COc1c(O)ccc2c1C(=O)c1c(O)cc(C)cc1C2=O`
ZINC13377961	0.594	322.3 Da LogP 3.44 TPSA 54.0	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccc2c(c1)OCO2)/C=C\c1ccc2c(c1)OCO2`
ZINC13481200	0.594	240.2 Da LogP 1.87 TPSA 74.6	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2c(O)cc(O)cc21`
ZINC152470	0.594	322.3 Da LogP 3.44 TPSA 54.0	✓ Ro5	✓ Clean	`O=C(/C=C/c1ccc2c(c1)OCO2)/C=C/c1ccc2c(c1)OCO2`
ZINC5698997	0.594	322.3 Da LogP 3.44 TPSA 54.0	✓ Ro5	✓ Clean	`O=C(/C=C\c1ccc2c(c1)OCO2)/C=C/c1ccc2c(c1)OCO2`
ZINC3055007	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`

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.