› 3dvb

X-ray diffraction
1.7Å resolution

X-ray crystal structure of mutant N62V human Carbonic Anhydrase II

Released:
DOI: 10.2210/pdb3dvb/pdb
PDB entry 3dvb coloured by chain, front view.
PDB entry 3dvb coloured by chain, side view.
PDB entry 3dvb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II.
Zheng J, Avvaru BS, Tu C, McKenna R, Silverman DN
Biochemistry 47 12028-36 (2008)
PMID: 18942852

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: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 29.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 42.795Å b: 41.696Å c: 72.927Å
α: 90° β: 104.64° γ: 90°
R-values:
R R work R free
0.184 0.184 0.197
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Thermodynamic, kinetic, and structural parameterization of human carbonic anhydrase interactions toward enhanced inhibitor design.
Linkuvienė et al. (2018)
3 more

1 mention without citation

Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II.
Zheng et al. (2008)