5thw

X-ray diffraction
2.5Å resolution

Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H(2)O = L-2-amino acid + NH(3) + CO(2)
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deacylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 434 amino acids
Theoretical weight: 46.95 KDa
Source organism: Burkholderia multivorans ATCC 17616
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3KRF1 (Residues: 1-426; Coverage: 100%)
Gene name: BMULJ_06149
Sequence domains: Peptidase family M20/M25/M40
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 86.46Å b: 88.51Å c: 126.44Å
α: 90° β: 90.21° γ: 90°
R-values:
R R work R free
0.156 0.155 0.212
Expression system: Escherichia coli BL21(DE3)