PDBe 2hfw

X-ray diffraction
2.5Å resolution

Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 3 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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
Spacegroup: P212121
Unit cell:
a: 42.373Å b: 51.674Å c: 117.659Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.239
Expression system: Escherichia coli BL21