PDBe 3eyx

X-ray diffraction
2.04Å resolution

Crystal structure of Carbonic Anhydrase Nce103 from Saccharomyces cerevisiae

Released:

Function and Biology Details

Reaction catalysed:
H(2)CO(3) = CO(2) + H(2)O. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 24.56 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53615 (Residues: 14-221; Coverage: 94%)
Gene names: N2695, NCE103, NCE3, YNL036W
Sequence domains: Carbonic anhydrase
Structure domains: Beta-carbonic Anhydrase; Chain A

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 60.57Å b: 155.73Å c: 89.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.241
Expression system: Escherichia coli