Protein profile

PA3758

N-acetylglucosamine-6-phosphate deacetylase

Genome: NC_002516.2

Gene: PA3758 Structure source: AlphaFold UniProt Q9HXN7

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Amino acids 363

Annotations 6

Features 16

PDB binders 0

Overview

Basic information about this protein and its source genome.

Accession: PA3758
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3758
Status: annotated
Amino acids: 363
Structure source: AlphaFold

GO:0046872 Binding to a metal ion. GO:0008448 Catalysis of the reaction: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate. GO:0006046 The chemical reactions and pathways resulting in the breakdown of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds. GO:0006044 The chemical reactions and pathways involving N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 36.19
Human E-value: 5.18e-11
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0046872 Binding to a metal ion.
GO:0008448 Catalysis of the reaction: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate.
GO:0006046 The chemical reactions and pathways resulting in the breakdown of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
GO:0006044 The chemical reactions and pathways involving N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records

Show feature table

Start	End	DB	Term	Name
4	362	PANTHER	PTHR11113	N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE
45	332	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
45	332	InterPro	IPR032466	Metal-dependent hydrolase
46	329	Gene3D	G3DSA:3.20.20.140	-
41	361	Pfam	PF01979	Amidohydrolase family
41	361	InterPro	IPR006680	Amidohydrolase-related
4	360	CDD	cd00854	NagA
4	360	InterPro	IPR003764	N-acetylglucosamine-6-phosphate deacetylase
5	360	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
5	360	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
3	362	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
3	362	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
3	363	PIRSF	PIRSF038994	NagA
3	363	InterPro	IPR003764	N-acetylglucosamine-6-phosphate deacetylase
40	360	NCBIfam	TIGR00221	N-acetylglucosamine-6-phosphate deacetylase
40	360	InterPro	IPR003764	N-acetylglucosamine-6-phosphate deacetylase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

No pockets are loaded yet for the displayed AlphaFold model PA3758 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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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 PA3758	AlphaFold	—	—	full sequence	—	Viewing

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.

41 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.

No PDB ligands found through similar proteins.

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
CHEMBL3219353	Q9Y303	7.47	337.2 Da LogP -2.69 TPSA 186.0	1 viol.	✓ Clean	`CP(=O)(O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](COP(=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
ZINC100350901	0.683	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	0.683	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	0.683	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	0.683	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	0.683	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	0.683	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	0.683	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	0.683	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	0.683	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](…`
ZINC12504154	0.639	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	0.639	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	0.639	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	0.639	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	0.639	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`
ZINC100351935	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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	0.622	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@…`
ZINC13516910	0.579	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	0.579	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	0.575	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	0.575	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@…`
ZINC56870785	0.564	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`
ZINC13513381	0.545	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	0.545	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…`
ZINC13522068	0.512	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	0.512	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	0.512	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@…`
ZINC12502703	0.500	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	0.500	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@@…`

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.