› 1o59

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reaction catalysed: 
Allantoate + H(2)O = (S)-ureidoglycolate + urea
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Allantoicase Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 40.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P25335 (Residues: 1-343; Coverage: 100%)
Gene names: ALC1, DAL2, YIR029W
Sequence domains: Allantoicase repeat
Structure domains: Galactose-binding domain-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1, SSRL BEAMLINE BL9-2
Spacegroup: P6322
Unit cell:
a: 107.209Å b: 107.209Å c: 134.918Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.175 0.222
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Crystal structure of ureidoglycolate hydrolase (AllA) from Escherichia coli O157:H7.
Raymond et al. (2005)
1 more