PDBe 3cq6

X-ray diffraction
2.1Å resolution

Histidinol-phosphate aminotransferase from Corynebacterium glutamicum holo-form (PLP covalently bound )

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, C, E
Molecule details ›
Chains: A, C, E
Length: 369 amino acids
Theoretical weight: 40.47 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli BL21(DE3)
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:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 191.798Å b: 80.017Å c: 88.484Å
α: 90° β: 94.79° γ: 90°
R-values:
R R work R free
0.2 0.198 0.238
Expression system: Escherichia coli BL21(DE3)