› 1koq

X-ray diffraction
1.9Å resolution

NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE

Released:
DOI: 10.2210/pdb1koq/pdb
PDB entry 1koq coloured by chain, front view.
PDB entry 1koq coloured by chain, side view.
PDB entry 1koq coloured by chain, top view.
Source organism: Neisseria gonorrhoeae
Primary publication:
Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide.
Huang S, Xue Y, Sauer-Eriksson E, Chirica L, Lindskog S, Jonsson BH
J Mol Biol 283 301-10 (1998)
PMID: 9761692

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175893 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 25.04 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q50940 (Residues: 30-252; Coverage: 99%)
Gene name: cah
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 47.23Å b: 74.94Å c: 62.38Å
α: 90° β: 93.87° γ: 90°
R-values:
R R work R free
0.206 0.206 0.271
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Prokaryotic carbonic anhydrases.
Smith et al. (2000)
4 more

8 mentions without citation

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