› 1yqc

X-ray diffraction
1.71Å resolution

Crystal Structure of Ureidoglycolate Hydrolase (AllA) from Escherichia coli O157:H7

Released:
DOI: 10.2210/pdb1yqc/pdb
PDB entry 1yqc coloured by chain, front view.
PDB entry 1yqc coloured by chain, side view.
PDB entry 1yqc coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Crystal structure of ureidoglycolate hydrolase (AllA) from Escherichia coli O157:H7.
Raymond S, Tocilj A, Ajamian E, Li Y, Hung MN, Matte A, Cygler M
Proteins 61 454-9 (2005)
PMID: 16114032

Function and Biology Details

Reaction catalysed: 
(S)-ureidoglycolate = glyoxylate + urea
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ureidoglycolate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 170 amino acids
Theoretical weight: 19.58 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P63486 (Residues: 1-160; Coverage: 100%)
Gene names: ECs0566, Z0659, allA
Sequence domains: Ureidoglycolate lyase
Structure domains: Ureidoglycolate hydrolase

Ligands and Environments

1 bound ligand:
Ligand GLV 1 x GLV
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21
Unit cell:
a: 43.047Å b: 74.466Å c: 56.364Å
α: 90° β: 103.894° γ: 90°
R-values:
R R work R free
0.228 0.226 0.269
Expression system: Escherichia coli

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Citations

1 review citation

New mechanisms for bacterial degradation of sulfoquinovose.
Wei et al. (2022)
4 other articles

3 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
2 more