› 2vvb

X-ray diffraction
1.66Å resolution

Human carbonic anhydrase II in complex with bicarbonate

Released:
DOI: 10.2210/pdb2vvb/pdb
PDB entry 2vvb coloured by chain, front view.
PDB entry 2vvb coloured by chain, side view.
PDB entry 2vvb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural study of X-ray induced activation of carbonic anhydrase.
Sjöblom B, Polentarutti M, Djinovic-Carugo K
Proc Natl Acad Sci U S A 106 10609-13 (2009)
PMID: 19520834

Function and Biology Details

Reactions catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Urea = cyanamide + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chain: X
Molecule details ›
Chain: X
Length: 260 amino acids
Theoretical weight: 29.29 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: Alpha carbonic anhydrase

Ligands and Environments

5 bound ligands:
Ligand SO4 2 x SO4
Ligand BCT 1 x BCT
Ligand CO2 1 x CO2
Ligand GOL 2 x GOL
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 42.667Å b: 41.653Å c: 72.91Å
α: 90° β: 104.79° γ: 90°
R-values:
R R work R free
0.171 0.168 0.213
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation.
Appel et al. (2013)
3 more

9 mentions without citation

Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.
Nocentini et al. (2021)
8 more