PDBe 1dca

X-ray diffraction
2.2Å resolution

STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH

Released:
Source organism: Homo sapiens

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.29 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Carbonic Anhydrase II

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 42.7Å b: 41.7Å c: 73Å
α: 90° β: 104.6° γ: 90°
R-values:
R R work R free
0.182 not available not available
Expression system: Not provided