PDBe 1z93

X-ray diffraction
2.1Å resolution

Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.

Released:

Function and Biology Details

Reaction catalysed:
H(2)CO(3) = CO(2) + H(2)O. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 3 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07451 (Residues: 1-260; Coverage: 100%)
Gene name: CA3
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Carbonic Anhydrase II

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P65
Unit cell:
a: 44.7Å b: 44.7Å c: 222.557Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.258
Expression system: Escherichia coli