2oof

X-ray diffraction
2.2Å resolution

The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from environmental sample

Released:
Source organism: unidentified
Entry authors: Tyagi R, Eswaramoorthy S, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H(2)O = N-formimidoyl-L-glutamate + H(+)
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-106095 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazolonepropionase Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 45.71 KDa
Source organism: unidentified
Expression system: Escherichia coli
UniProt:
  • Canonical: A0KF84 (Residues: 6-411; Coverage: 99%)
Gene names: AHA_0377, hutI
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P3221
Unit cell:
a: 95.851Å b: 95.851Å c: 115.931Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.225
Expression system: Escherichia coli