1xsq

X-ray diffraction
1.6Å resolution

Crystal structure of ureidoglycolate hydrolase from E.coli. Northeast Structural Genomics Consortium target ET81.

Released:
Source organism: Escherichia coli
Entry authors: Kuzin AP, Vorobiev SM, Abashidze M, Acton TB, Ma L-C, Xiao R, Montelione GT, Hunt JF, Tong L, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

Reaction catalysed:
(S)-ureidoglycolate = glyoxylate + urea
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160193 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ureidoglycolate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 19.35 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77731 (Residues: 1-160; Coverage: 100%)
Gene names: JW0493, allA, b0505, glxA2, ybbT
Sequence domains: Ureidoglycolate lyase
Structure domains: Ureidoglycolate hydrolase

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 43.194Å b: 45.273Å c: 51.801Å
α: 100.7° β: 99.84° γ: 117.19°
R-values:
R R work R free
0.227 0.227 0.257
Expression system: Escherichia coli