› 2h4n

X-ray diffraction
1.9Å resolution

H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE

Released:
DOI: 10.2210/pdb2h4n/pdb
PDB entry 2h4n coloured by chain, front view.
PDB entry 2h4n coloured by chain, side view.
PDB entry 2h4n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity.
Lesburg CA, Huang C, Christianson DW, Fierke CA
Biochemistry 36 15780-91 (1997)
PMID: 9398308

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: 259 amino acids
Theoretical weight: 29.13 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

2 bound ligands:
Ligand ZN 2 x ZN
Ligand AZM 1 x AZM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
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
0.177 0.177 0.219
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

6 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
5 more