Protein profile

KP13_03771

Imidazole glycerol phosphate synthase subunit hisH

Genome: KpKP13

Gene: hisH AHE43692.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GSH1
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Amino acids 196
Annotations 8
Features 20
PDB binders 1
Druggability 0.516

Overview

Basic information about this protein and its source genome.

Accession
KP13_03771
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
hisH AHE43692.1
Status
annotated
Amino acids
196
Structure source
AlphaFold + ColabFold
EC
4.3.2.10 3.5.1.2
GO
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor). GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
41.709
DEG E-value
3.02e-48
Localization
Cytoplasmic
ColabFold pLDDT
96.94

Selected Druggability evidence

AlphaFold / UniProt model

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 0.516
Structure A0A0H3GSH1
Pocket Pocket 6
P2Rank 0.188
Structure A0A0H3GSH1
Pocket Pocket 1
ColabFold model
FPocket 0.379 · Pocket 5
P2Rank 0.189 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 168 / 4744 genomes with a hit
Normalized 0.035

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 6 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

6
  • GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
  • GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0004359 Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH4+.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
3 194 CDD cd01748 GATase1_IGP_Synthase
3 194 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
2 196 ProSiteProfiles PS51273 Glutamine amidotransferase type 1 domain profile.
38 194 Pfam PF00117 Glutamine amidotransferase class-I
38 194 InterPro IPR017926 Glutamine amidotransferase
1 196 PIRSF PIRSF000495 Amidotransf_HisH
1 196 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
1 196 Gene3D G3DSA:3.40.50.880 -
1 196 InterPro IPR029062 Class I glutamine amidotransferase-like
2 196 Hamap MF_00278 Imidazole glycerol phosphate synthase subunit HisH [hisH].
2 196 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
2 195 PANTHER PTHR42701 IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH
2 195 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
1 196 FunFam G3DSA:3.40.50.880:FF:000009 Imidazole glycerol phosphate synthase subunit HisH
174 187 PRINTS PR00096 Glutamine amidotransferase superfamily signature
72 83 PRINTS PR00096 Glutamine amidotransferase superfamily signature
3 196 NCBIfam TIGR01855 imidazole glycerol phosphate synthase subunit HisH
3 196 InterPro IPR010139 Imidazole glycerol phosphate synthase, subunit H
3 195 SUPERFAMILY SSF52317 Class I glutamine amidotransferase-like
3 195 InterPro IPR029062 Class I glutamine amidotransferase-like

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 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GSH1
AlphaFold — — full sequence — Viewing
ColabFold KP13_03771
ColabFold — — full sequence — Loaded
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
6 0.516
3 0.247

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 2.74 0.083

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.

51 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
GUO
7AC8
Q9X0C8 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…

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.