2ivq

X-ray diffraction
2.1Å resolution

SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE

Released:
Source organism: Escherichia coli
Entry authors: Guilloton M, Walsh MA, Joachimiak A, Anderson PM

Function and Biology Details

Reaction catalysed:
(1a) cyanate + HCO(3)(-) + H(+) = carbamate + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133602 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyanate hydratase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 156 amino acids
Theoretical weight: 17.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00816 (Residues: 1-156; Coverage: 100%)
Gene names: JW0331, b0340, cnt, cynS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 76.883Å b: 80.845Å c: 82.647Å
α: 69.99° β: 71.98° γ: 66.17°
R-values:
R R work R free
0.183 0.18 0.243
Expression system: Escherichia coli