› 4cqc

X-ray diffraction
2.2Å resolution

The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies

Released:
DOI: 10.2210/pdb4cqc/pdb
PDB entry 4cqc coloured by chain, front view.
PDB entry 4cqc coloured by chain, side view.
PDB entry 4cqc coloured by chain, top view.
Source organism: Pseudomonas sp. ADP
Primary publication:
X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.
Balotra S, Warden AC, Newman J, Briggs LJ, Scott C, Peat TS
PLoS One 10 e0137700 (2015)
PMID: 26390431

Function and Biology Details

Reaction catalysed: 
N-isopropylammelide + H(2)O = cyanuric acid + isopropylamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129370 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-isopropylammelide isopropyl amidohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 423 amino acids
Theoretical weight: 47.1 KDa
Source organism: Pseudomonas sp. ADP
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O52063 (Residues: 1-403; Coverage: 100%)
Gene name: atzC
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand CL 2 x CL
Ligand EPE 2 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2
Unit cell:
a: 106.234Å b: 87.28Å c: 114.364Å
α: 90° β: 103.93° γ: 90°
R-values:
R R work R free
0.197 0.196 0.223
Expression system: Escherichia coli BL21

Quick links

Citations

2 citation in other articles

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.
Esquirol et al. (2018)
1 more

1 mention without citation

X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.
Balotra et al. (2015)