› 3cq4

X-ray diffraction
2.2Å resolution

Histidinol-phosphate aminotransferase from Corynebacterium glutamicum

Released:
DOI: 10.2210/pdb3cq4/pdb
PDB entry 3cq4 coloured by chain, front view.
PDB entry 3cq4 coloured by chain, side view.
PDB entry 3cq4 coloured by chain, top view.
Source organism: Corynebacterium glutamicum
Primary publication:
Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum.
Marienhagen J, Sandalova T, Sahm H, Eggeling L, Schneider G
Acta Crystallogr D Biol Crystallogr 64 675-85 (2008)
PMID: 18560156

Function and Biology Details

Reaction catalysed: 
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191908 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 376 amino acids
Theoretical weight: 41.16 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KJU4 (Residues: 1-366; Coverage: 100%)
Gene names: Cgl2101, cg2304, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3221
Unit cell:
a: 102.34Å b: 102.34Å c: 140.108Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.237 0.277
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.
Kulis-Horn et al. (2014)
6 other articles