Protein profile

PA5140

imidazole glycerol phosphate synthase subunit HisF

Genome: NC_002516.2

Gene: PA5140 hisF1 Structure source: AlphaFold UniProt Q9HU44
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Amino acids 256
Annotations 5
Features 14
PDB binders 7
Druggability 0.605

Overview

Basic information about this protein and its source genome.

Accession
PA5140
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5140 hisF1
Status
annotated
Amino acids
256
Structure source
AlphaFold
EC
4.3.2.10
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0000107 Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+. GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.605
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0000107 Catalysis of the reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + aminoimidazole carboxamide ribonucleotide + L-glutamate + 2 H+.
  • GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
  • GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
2 256 Hamap MF_01013 Imidazole glycerol phosphate synthase subunit HisF [hisF].
2 256 InterPro IPR004651 Histidine biosynthesis, HisF
3 256 NCBIfam TIGR00735 imidazole glycerol phosphate synthase subunit HisF
3 256 InterPro IPR004651 Histidine biosynthesis, HisF
5 251 CDD cd04731 HisF
5 251 InterPro IPR004651 Histidine biosynthesis, HisF
3 256 SUPERFAMILY SSF51366 Ribulose-phoshate binding barrel
3 256 InterPro IPR011060 Ribulose-phosphate binding barrel
6 240 Pfam PF00977 Histidine biosynthesis protein
6 240 InterPro IPR006062 Histidine biosynthesis protein
1 256 Gene3D G3DSA:3.20.20.70 Aldolase class I
1 256 InterPro IPR013785 Aldolase-type TIM barrel
1 256 FunFam G3DSA:3.20.20.70:FF:000006 Imidazole glycerol phosphate synthase subunit HisF
2 256 PANTHER PTHR21235 IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H

3D Structure

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

3D visualization script Full viewer

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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 PA5140
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 0.605
2 0.261

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

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
0VR
4EWN
Q9X0C6 351.2 Da LogP -1.01 TPSA 176.8 1 viol. ✓ Clean c1ccc(c(c1)C(=O)O)NC[C@@H]([C@@H]([C@@H](COP(=O…
137
2Y85
P9WMM5 351.2 Da LogP -1.01 TPSA 176.8 1 viol. ✓ Clean c1ccc(c(c1)C(=O)O)NC[C@H]([C@@H]([C@@H](COP(=O)…
1PR
1OX5
P33734 581.4 Da LogP -5.14 TPSA 328.9 3 viol. ✓ Clean c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…
2ER
5AB3
P10372 577.3 Da LogP -4.45 TPSA 326.0 3 viol. ✓ Clean c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…
CXS
4X2R
C0W7K4 221.3 Da LogP 1.19 TPSA 66.4 ✓ Ro5 ✓ Clean C1CCC(CC1)NCCCS(=O)(=O)O
GUO
5A5W
P10372 577.3 Da LogP -4.48 TPSA 318.2 3 viol. ✓ Clean c1nc(c(n1[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O…
POP
1JVN
P33734 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.