PDBe 1dw9

X-ray diffraction
1.65Å resolution

Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site

Released:

Function and Biology Details

Reaction catalysed:
Cyanate + HCO(3)(-) + 2 H(+) = NH(3) + 2 CO(2). 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo decamer (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: 17.26 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: Cyanate lyase C-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 76.34Å b: 81.03Å c: 82.3Å
α: 70.3° β: 72.2° γ: 66.4°
R-values:
R R work R free
0.15 0.15 0.189
Expression system: Escherichia coli