PDBe 1cvh

X-ray diffraction
2.3Å resolution

STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE

Released:
Source organism: Homo sapiens
Primary publication:
Structural consequences of redesigning a protein-zinc binding site.
Biochemistry 33 15241-9 (1994)
PMID: 7803386

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: 255 amino acids
Theoretical weight: 28.63 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 5-259; Coverage: 98%)
Gene name: CA2
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