5l9e

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER

Released:
Source organism: Homo sapiens
Entry authors: Vallade M, Langlois d'Estaintot B, Granier T, Huc I

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 260 amino acids
Theoretical weight: 29.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Unit cell:
a: 125.972Å b: 75.14Å c: 141.098Å
α: 90° β: 100.08° γ: 90°
R-values:
R R work R free
0.244 0.242 0.273
Expression system: Escherichia coli BL21(DE3)