› 1cvd

X-ray diffraction
2.2Å resolution

STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE

Released:
DOI: 10.2210/pdb1cvd/pdb
PDB entry 1cvd coloured by chain, front view.
PDB entry 1cvd coloured by chain, side view.
PDB entry 1cvd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural consequences of redesigning a protein-zinc binding site.
Ippolito JA, Christianson DW
Biochemistry 33 15241-9 (1994)
PMID: 7803386

Function and Biology Details

Reactions catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Urea = cyanamide + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chain: A
Molecule details ›
Chain: A
Length: 255 amino acids
Theoretical weight: 28.63 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 5-259; Coverage: 98%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
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
0.184 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Neuronal CA2+/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function.
Hudmon et al. (2002)
8 more