› 2cab

X-ray diffraction
2Å resolution

STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I

Released:
DOI: 10.2210/pdb2cab/pdb
PDB entry 2cab coloured by chain, front view.
PDB entry 2cab coloured by chain, side view.
PDB entry 2cab coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I.
Kannan KK, Ramanadham M, Jones TA
Ann N Y Acad Sci 429 49-60 (1984)
PMID: 6430186

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-133680 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 1 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 28.79 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00915 (Residues: 2-261; Coverage: 100%)
Gene name: CA1
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
Spacegroup: P212121
Unit cell:
a: 81.5Å b: 73.6Å c: 37.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 not available
Expression system: Not provided

Quick links

Citations

12 review citations

Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulations.
Swanson et al. (2007)
11 more

19 mentions without citation

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