› 1cim

X-ray diffraction
2.1Å resolution

THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS

Released:
DOI: 10.2210/pdb1cim/pdb
PDB entry 1cim coloured by chain, front view.
PDB entry 1cim coloured by chain, side view.
PDB entry 1cim coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors.
Smith GM, Alexander RS, Christianson DW, McKeever BM, Ponticello GS, Springer JP, Randall WC, Baldwin JJ, Habecker CN
Protein Sci 3 118-25 (1994)
PMID: 8142888

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: 259 amino acids
Theoretical weight: 29.16 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: Alpha carbonic anhydrase

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand MMC 1 x MMC
Ligand PTS 1 x PTS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 42.72Å b: 41.93Å c: 72.69Å
α: 90° β: 104.77° γ: 90°
Expression system: Not provided

Quick links

Citations

5 review citations

Structure and mechanism of carbonic anhydrase.
Lindskog S. (1997)
4 more

11 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
10 more