3ftb

X-ray diffraction
2Å resolution

The crystal structure of the histidinol-phosphate aminotransferase from Clostridium acetobutylicum

Released:
Source organism: Clostridium acetobutylicum
Entry authors: Zhang R, Bigelow L, Moy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotran_1_2 domain-containing protein Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 361 amino acids
Theoretical weight: 41.22 KDa
Source organism: Clostridium acetobutylicum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97JB7 (Residues: 1-361; Coverage: 100%)
Gene names: CA_C1369, 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: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 66.556Å b: 121.663Å c: 94.185Å
α: 90° β: 90.09° γ: 90°
R-values:
R R work R free
0.176 0.174 0.212
Expression system: Escherichia coli