PDBe 4cp8

X-ray diffraction
2.5Å resolution

Structure of the amidase domain of allophanate hydrolase from Pseudomonas sp strain ADP

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Allophanate hydrolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 487 amino acids
Theoretical weight: 51.93 KDa
Source organism: Pseudomonas sp. ADP
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q936X2 (Residues: 1-467; Coverage: 77%)
Gene name: atzF
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 82.447Å b: 179.232Å c: 112.61Å
α: 90° β: 106.63° γ: 90°
R-values:
R R work R free
0.226 0.224 0.259
Expression system: Escherichia coli BL21