PDBe 3cq4

X-ray diffraction
2.2Å resolution

Histidinol-phosphate aminotransferase from Corynebacterium glutamicum

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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:

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