PDBe 1ccu

X-ray diffraction
2.25Å resolution

STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY

Released:
Source organism: Homo sapiens
Primary publication:
Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity.
Proc. Natl. Acad. Sci. U.S.A. 92 5017-21 (1995)
PMID: 7761440

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 2 Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 29.19 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 2-260; Coverage: 100%)
Gene name: CA2
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
Spacegroup: P21
Unit cell:
a: 42.7Å b: 41.7Å c: 73Å
α: 90° β: 104.6° γ: 90°
R-values:
R R work R free
0.178 not available not available
Expression system: Not provided