3lhl

X-ray diffraction
2.3Å resolution

Crystal structure of a putative agmatinase from Clostridium difficile

Released:
Source organism: Clostridioides difficile 630
Entry authors: Palani K, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
PDBe Complex ID:
PDB-CPX-172726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Agmatinase (Agmatine ureohydrolase) (AUH) Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 32.9 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q18A84 (Residues: 17-292; Coverage: 95%)
Gene names: CD630_08910, speB
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P6322
Unit cell:
a: 77.35Å b: 77.35Å c: 166.118Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.238
Expression system: Escherichia coli BL21(DE3)