› 1ysd

X-ray diffraction
1.9Å resolution

Yeast Cytosine Deaminase Double Mutant

Released:
DOI: 10.2210/pdb1ysd/pdb
PDB entry 1ysd coloured by chain, front view.
PDB entry 1ysd coloured by chain, side view.
PDB entry 1ysd coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Computational thermostabilization of an enzyme.
Korkegian A, Black ME, Baker D, Stoddard BL
Science 308 857-60 (2005)
PMID: 15879217

Function and Biology Details

Reaction catalysed: 
Cytosine + H(2)O = uracil + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosine deaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 161 amino acids
Theoretical weight: 17.8 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12178 (Residues: 1-158; Coverage: 100%)
Gene names: FCY1, YP9499.17, YPR062W
Sequence domains: Cytidine and deoxycytidylate deaminase zinc-binding region
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 39.35Å b: 54.77Å c: 68.4Å
α: 90° β: 105.68° γ: 90°
R-values:
R R work R free
0.163 0.163 0.2
Expression system: Escherichia coli

Quick links

Citations

41 review citations

Deconstruction of lignocellulosic biomass to fuels and chemicals.
Chundawat et al. (2011)
40 more

1 mention without citation

Computational thermostabilization of an enzyme.
Korkegian et al. (2005)