› 2q09

X-ray diffraction
1.97Å resolution

Crystal structure of Imidazolonepropionase from environmental sample with bound inhibitor 3-(2,5-Dioxo-imidazolidin-4-yl)-propionic acid

Released:
DOI: 10.2210/pdb2q09/pdb
PDB entry 2q09 coloured by chain, front view.
PDB entry 2q09 coloured by chain, side view.
PDB entry 2q09 coloured by chain, top view.
Source organism: unidentified
Primary publication:
A common catalytic mechanism for proteins of the HutI family.
Tyagi R, Eswaramoorthy S, Burley SK, Raushel FM, Swaminathan S
Biochemistry 47 5608-15 (2008)
PMID: 18442260

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:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

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 BL21(DE3)
UniProt:
  • Canonical: A0KF84 (Residues: 6-411; Coverage: 99%)
Gene names: AHA_0377, hutI
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand DI6 1 x DI6
1 modified residue:
Ligand MSE 11 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P3221
Unit cell:
a: 95.91Å b: 95.91Å c: 115.473Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.194 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Regulation of the histidine utilization (hut) system in bacteria.
Bender RA. (2012)
1 more

3 mentions without citation

Ligands in PSI structures.
Kumar et al. (2010)
2 more