› 2imo

X-ray diffraction
2.8Å resolution

Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6

Released:
DOI: 10.2210/pdb2imo/pdb
PDB entry 2imo coloured by chain, front view.
PDB entry 2imo coloured by chain, side view.
PDB entry 2imo coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics.
Agarwal R, Burley SK, Swaminathan S
J Mol Biol 368 450-63 (2007)
PMID: 17362992

Function and Biology Details

Reaction catalysed: 
Allantoate + H(2)O = (S)-ureidoglycine + NH(3) + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Allantoate amidohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 423 amino acids
Theoretical weight: 47.76 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77425 (Residues: 2-411; Coverage: 100%)
Gene names: JW0504, allC, b0516, glxB7, ylbB
Sequence domains: Peptidase family M20/M25/M40
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 28 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 94.747Å b: 183.923Å c: 48.777Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.245 0.302
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Carbamoylases: characteristics and applications in biotechnological processes.
Martínez-Rodríguez et al. (2010)
1 more

2 mentions without citation

Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.
Martínez-Rodríguez et al. (2012)
1 more