› 1fqr

X-ray diffraction
2Å resolution

X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT

Released:
DOI: 10.2210/pdb1fqr/pdb
PDB entry 1fqr coloured by chain, front view.
PDB entry 1fqr coloured by chain, side view.
PDB entry 1fqr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II.
Cox JD, Hunt JA, Compher KM, Fierke CA, Christianson DW
Biochemistry 39 13687-94 (2000)
PMID: 11076507

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: 29.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 42Å b: 42.3Å c: 72.4Å
α: 90° β: 103.1° γ: 90°
R-values:
R R work R free
0.216 0.216 0.275
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

The Loss and Gain of Functional Amino Acid Residues Is a Common Mechanism Causing Human Inherited Disease.
Lugo-Martinez et al. (2016)