X-ray diffraction
1.8Å resolution

Histidinol-phosphate aminotransferase from Corynebacterium glutamicum in complex with PMP

Source organism: Corynebacterium glutamicum
Entry authors: Sandalova T, Marienhagen J, Schneider G

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Histidinol-phosphate aminotransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 369 amino acids
Theoretical weight: 40.24 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9KJU4 (Residues: 1-366; Coverage: 100%)
Gene names: Cgl2101, cg2304, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

Cofactor: Ligand PMP 3 x PMP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 195.273Å b: 85.531Å c: 89.431Å
α: 90° β: 93.65° γ: 90°
R R work R free
0.193 0.192 0.219
Expression system: Escherichia coli BL21(DE3)