2ef4

X-ray diffraction
2.3Å resolution

Crystal structure of the arginase from thermus thermophilus

Released:
Source organism: Thermus thermophilus
Entry authors: Kumarevel TS, Karthe P, Kuramitsu S, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
L-arginine + H(2)O = L-ornithine + urea
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 31.14 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SI78 (Residues: 2-291; Coverage: 100%)
Gene name: TTHA1496
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P4232
Unit cell:
a: 121.572Å b: 121.572Å c: 121.572Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.254 0.259
Expression system: Escherichia coli