2hvw

X-ray diffraction
1.67Å resolution

Crystal structure of dCMP deaminase from Streptococcus mutans

Released:

Function and Biology Details

Reaction catalysed:
dCMP + H(2)O = dUMP + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-184177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CMP/dCMP-type deaminase domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 184 amino acids
Theoretical weight: 20.41 KDa
Source organism: Streptococcus mutans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8DSE5 (Residues: 1-150; Coverage: 100%)
Gene names: SMU_1849, comEB
Sequence domains: Cytidine and deoxycytidylate deaminase zinc-binding region
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 95.498Å b: 99.657Å c: 141.388Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.149 0.179
Expression system: Escherichia coli BL21(DE3)