› 1uu2

X-ray diffraction
2.8Å resolution

Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (apo-form)

Released:
DOI: 10.2210/pdb1uu2/pdb
PDB entry 1uu2 coloured by chain, front view.
PDB entry 1uu2 coloured by chain, side view.
PDB entry 1uu2 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.
Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M
J Biol Chem 279 21478-88 (2004)
PMID: 15007066

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidinol-phosphate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 39.35 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X0D0 (Residues: 1-335; Coverage: 100%)
Gene names: TM_1040, hisC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 2 x PMP
1 bound ligand:
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 54.646Å b: 98.56Å c: 124.585Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.288
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
1 more