PDBe 3v3h

X-ray diffraction
1.85Å resolution

Kinetic and structural studies of thermostabilized mutants of HCA II.

Released:

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: B
Molecule details ›
Chain: B
Length: 260 amino acids
Theoretical weight: 29.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 42.165Å b: 71.893Å c: 74.576Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.165 0.224
Expression system: Escherichia coli