Protein profile

PA1002

anthranilate synthase component II

Genome: NC_002516.2

Gene: PA1002 trpG phnB Structure source: AlphaFold UniProt P09786
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Amino acids 200
Annotations 5
Features 23
PDB binders 1
Druggability 0.406

Overview

Basic information about this protein and its source genome.

Accession
PA1002
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1002 trpG phnB
Status
annotated
Amino acids
200
Structure source
AlphaFold
EC
4.1.3.27
GO
GO:0004048 Catalysis of the reaction: N-(5-phospho-beta-D-ribosyl)anthranilate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate. GO:0004049 Catalysis of the reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. GO:0000162 The chemical reactions and pathways resulting in the formation of L-tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; L-tryptophan is synthesized from chorismate via anthranilate. GO:0002047 The chemical reactions and pathways resulting in the formation of a phenazine antibiotic, a polycyclic pyrazine with two nitrogen atoms in the ring.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
29.814
Human E-value
6.42e-09
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 0.406
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0004048 Catalysis of the reaction: N-(5-phospho-beta-D-ribosyl)anthranilate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate.
  • GO:0004049 Catalysis of the reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
  • GO:0000162 The chemical reactions and pathways resulting in the formation of L-tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; L-tryptophan is synthesized from chorismate via anthranilate.
  • GO:0002047 The chemical reactions and pathways resulting in the formation of a phenazine antibiotic, a polycyclic pyrazine with two nitrogen atoms in the ring.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
78 89 PRINTS PR00096 Glutamine amidotransferase superfamily signature
165 178 PRINTS PR00096 Glutamine amidotransferase superfamily signature
51 60 PRINTS PR00096 Glutamine amidotransferase superfamily signature
1 190 Gene3D G3DSA:3.40.50.880 -
1 190 InterPro IPR029062 Class I glutamine amidotransferase-like
1 189 SUPERFAMILY SSF52317 Class I glutamine amidotransferase-like
1 189 InterPro IPR029062 Class I glutamine amidotransferase-like
3 186 CDD cd01743 GATase1_Anthranilate_Synthase
3 186 InterPro IPR006221 Anthranilate synthase/para-aminobenzoate synthase like domain
1 190 FunFam G3DSA:3.40.50.880:FF:000003 Anthranilate synthase component II
3 17 PRINTS PR00097 Anthranilate synthase component II signature
165 178 PRINTS PR00097 Anthranilate synthase component II signature
51 60 PRINTS PR00097 Anthranilate synthase component II signature
123 135 PRINTS PR00097 Anthranilate synthase component II signature
78 89 PRINTS PR00097 Anthranilate synthase component II signature
103 111 PRINTS PR00097 Anthranilate synthase component II signature
5 186 Pfam PF00117 Glutamine amidotransferase class-I
5 186 InterPro IPR017926 Glutamine amidotransferase
2 195 ProSiteProfiles PS51273 Glutamine amidotransferase type 1 domain profile.
78 94 PRINTS PR00099 Carbamoyl-phosphate synthase protein GATase domain signature
48 62 PRINTS PR00099 Carbamoyl-phosphate synthase protein GATase domain signature
3 186 NCBIfam TIGR00566 glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase
2 190 PANTHER PTHR43418 MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-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 PA1002
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
8 0.406
1 0.388
3 0.279

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.

18 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
POP
1GPM
P04079 176.0 Da LogP -2.08 TPSA 129.9 ✓ Ro5 ✓ Clean O[P@@](=O)([O-])O[P@@](=O)(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.