› 4gyr

X-ray diffraction
2.8Å resolution

Granulibacter bethesdensis allophanate hydrolase apo

Released:
DOI: 10.2210/pdb4gyr/pdb
PDB entry 4gyr coloured by chain, front view.
PDB entry 4gyr coloured by chain, side view.
PDB entry 4gyr coloured by chain, top view.
Source organism: Granulibacter bethesdensis CGDNIH1
Primary publication:
The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family.
Lin Y, St Maurice M
Biochemistry 52 690-700 (2013)
PMID: 23282241

Function and Biology Details

Reaction catalysed: 
Urea-1-carboxylate + H(2)O = 2 CO(2) + 2 NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170867 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 621 amino acids
Theoretical weight: 66.54 KDa
Source organism: Granulibacter bethesdensis CGDNIH1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0BRB0 (Residues: 1-592; Coverage: 100%)
Gene name: GbCGDNIH1_1744
Sequence domains: Amidase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P61
Unit cell:
a: 78.094Å b: 78.094Å c: 397.543Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.259 0.256 0.307
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Solving the Conundrum: Widespread Proteins Annotated for Urea Metabolism in Bacteria Are Carboxyguanidine Deiminases Mediating Nitrogen Assimilation from Guanidine.
Schneider et al. (2020)
9 more

2 mentions without citation

The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family.
Lin et al. (2013)
1 more