PDBe 1jd0

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CARBONIC ANHYDRASE XII COMPLEXED WITH ACETAZOLAMIDE

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 12 Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O43570 (Residues: 29-291; Coverage: 80%)
Gene name: CA12
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Carbonic Anhydrase II

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 146.875Å b: 45.08Å c: 85.232Å
α: 90° β: 93.98° γ: 90°
R-values:
R R work R free
0.19 0.19 0.207
Expression system: Escherichia coli BL21(DE3)