› 3cq5

X-ray diffraction
1.8Å resolution

Histidinol-phosphate aminotransferase from Corynebacterium glutamicum in complex with PMP

Released:
DOI: 10.2210/pdb3cq5/pdb
PDB entry 3cq5 coloured by chain, front view.
PDB entry 3cq5 coloured by chain, side view.
PDB entry 3cq5 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, 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)
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


Cofactor: Ligand PMP 3 x PMP
2 bound ligands:
Ligand SO4 6 x SO4
Ligand 144 3 x 144
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-values:
R R work R free
0.193 0.192 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

3 mentions without citation

Forcefield_PTM: Ab Initio Charge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications.
Khoury et al. (2013)
2 more