Protein profile

PA5439

glucose-6-phosphate 1-dehydrogenase

Genome: NC_002516.2

Gene: zwf PA5439 Structure source: AlphaFold UniProt Q9HTC7

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Amino acids 488

Annotations 7

Features 29

PDB binders 2

Druggability 0.875

Overview

Basic information about this protein and its source genome.

Accession: PA5439
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: zwf PA5439
Status: annotated
Amino acids: 488
Structure source: AlphaFold

1.1.1.49

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004345 Catalysis of the reaction: D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. GO:0009051 The branch of the pentose-phosphate shunt which involves the oxidation of glucose 6-P and produces ribulose 5-P, reduced NADP+ and carbon dioxide (CO2). 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 39.173
Human E-value: 2.9900000000000006e-86
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 0.875

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.1.1.49

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004345 Catalysis of the reaction: D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
GO:0009051 The branch of the pentose-phosphate shunt which involves the oxidation of glucose 6-P and produces ribulose 5-P, reduced NADP+ and carbon dioxide (CO2).
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
178	476	Gene3D	G3DSA:3.30.360.10	Dihydrodipicolinate Reductase; domain 2
8	485	PANTHER	PTHR23429	GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD
8	485	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
1	488	PIRSF	PIRSF000110	G6PD
1	488	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
9	488	Hamap	MF_00966	Glucose-6-phosphate 1-dehydrogenase [zwf].
9	488	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
329	355	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
329	355	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
238	254	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
238	254	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
144	157	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
144	157	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
220	237	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
220	237	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
168	196	PRINTS	PR00079	Glucose-6-phosphate dehydrogenase signature
168	196	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
190	486	Pfam	PF02781	Glucose-6-phosphate dehydrogenase, C-terminal domain
190	486	InterPro	IPR022675	Glucose-6-phosphate dehydrogenase, C-terminal
178	184	ProSitePatterns	PS00069	Glucose-6-phosphate dehydrogenase active site.
178	184	InterPro	IPR019796	Glucose-6-phosphate dehydrogenase, active site
12	436	Gene3D	G3DSA:3.40.50.720	-
5	191	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
5	191	InterPro	IPR036291	NAD(P)-binding domain superfamily
14	188	Pfam	PF00479	Glucose-6-phosphate dehydrogenase, NAD binding domain
14	188	InterPro	IPR022674	Glucose-6-phosphate dehydrogenase, NAD-binding
9	486	NCBIfam	TIGR00871	glucose-6-phosphate dehydrogenase
9	486	InterPro	IPR001282	Glucose-6-phosphate dehydrogenase
178	487	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain

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 PA5439	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
5				0.875
1				0.669
2				0.339

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.

52 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
BG6	7E6I	P48828	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O…`
GOA	1QKI	P11413	76.1 Da LogP -0.94 TPSA 57.5	✓ Ro5	✓ Clean	`C(C(=O)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
ZINC100351935	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@…`
ZINC1529564	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@…`
ZINC1532533	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC1532857	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC3581460	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…`
ZINC38276879	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC38276880	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H…`
ZINC3869397	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C…`
ZINC3875374	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC3875375	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@…`
ZINC4095545	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…`
ZINC4095546	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H…`
ZINC4096188	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@…`
ZINC8551507	1.000	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…`
ZINC12504154	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H]1O`
ZINC1532546	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H]1O`
ZINC4096190	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O`
ZINC4228241	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O`
ZINC4521831	0.962	230.1 Da LogP -2.47 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC13516910	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O`
ZINC2562340	0.733	244.1 Da LogP -2.42 TPSA 136.7	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O`
ZINC4097102	0.719	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC4097103	0.719	259.2 Da LogP -3.14 TPSA 162.7	1 viol.	✓ Clean	`N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC12502703	0.667	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC4095589	0.667	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC15298193	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262384	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262385	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@H…`
ZINC1933262386	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H]…`
ZINC1933262387	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H]…`
ZINC256073272	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H…`
ZINC256073273	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@…`
ZINC256073274	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@H…`
ZINC256073275	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[C@@H]2O[C@H](CO)[C@@…`
ZINC4228300	0.657	422.3 Da LogP -5.28 TPSA 236.1	2 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[C@H]2O[C@H](CO)[C@@H]…`
ZINC56870785	0.656	228.1 Da LogP -1.40 TPSA 116.5	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]1O`
ZINC13522068	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC3870205	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@@H](O)[C…`
ZINC4095560	0.636	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC13513381	0.622	301.2 Da LogP -2.12 TPSA 169.3	1 viol.	✓ Clean	`C/C(O)=N/[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@H]…`
ZINC30725927	0.622	301.2 Da LogP -2.12 TPSA 169.3	1 viol.	✓ Clean	`C/C(O)=N/[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@H…`
ZINC100350901	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@H](…`
ZINC1530414	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@@H](O)O[C@@H](COP(=O)(O)O)[C@H…`
ZINC1532625	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@@H](O)[C@H](COP(=O)(O)O…`
ZINC245204467	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@@H](O)[C@@H](COP(=O)(O)…`
ZINC245204468	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)[C@H](O)[C@@H](COP(=O)(O)O…`
ZINC30725207	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4096363	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H…`
ZINC4097100	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC4097101	0.605	301.2 Da LogP -2.96 TPSA 165.8	1 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[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.