› 4q0l

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129003 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 12 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 29.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43570 (Residues: 30-291; Coverage: 79%)
Gene name: CA12
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand V14 4 x V14
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 46.52Å b: 75.211Å c: 77.888Å
α: 109.42° β: 101.6° γ: 107.95°
R-values:
R R work R free
0.27 0.264 0.328
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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)
5 more

1 mention without citation

Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.
Smirnov et al. (2018)