1woh

X-ray diffraction
1.75Å resolution

Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

Released:

Function and Biology Details

Reaction catalysed:
Agmatine + H(2)O = putrescine + urea
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193363 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Agmatinase, putative Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 305 amino acids
Theoretical weight: 32.67 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RZ04 (Residues: 1-304; Coverage: 100%)
Gene name: DR_A0149
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: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 81.877Å b: 130.537Å c: 168.644Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.248
Expression system: Escherichia coli