› 2cba

X-ray diffraction
1.54Å resolution

STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES

Released:
DOI: 10.2210/pdb2cba/pdb
PDB entry 2cba coloured by chain, front view.
PDB entry 2cba coloured by chain, side view.
PDB entry 2cba coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes.
Håkansson K, Carlsson M, Svensson LA, Liljas A
J Mol Biol 227 1192-204 (1992)
PMID: 1433293

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 domain:

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: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.18 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 2-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
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
0.151 not available not available
Expression system: Not provided

Quick links

Citations

20 review citations

Calcineurin: form and function.
Rusnak et al. (2000)
19 more

71 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
70 more