2ez7 Summary


Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII and XIV with L- and D-histidine and crystallographic analysis of their adducts with isoform II: engineering proton transfer processes within the active site of an enzyme

The structure was published by Temperini, C., Scozzafava, A., Vullo, D., and Supuran, C.T., in 2006 in a paper entitled "Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, VA, VII, and XIV with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton-Transfer Processes within the Active Site of an Enzyme." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Carbonic anhydrase 2. This molecule has the UniProt identifier P00918 (CAH2_HUMAN)search. The sample contained 260 residues which is 100% of the natural sequence. Out of 260 residues 258 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Carbonic anhydrase 2 P00918 (1-259) (CAH2_HUMAN)search Homo sapienssearch 98% 260 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00918 (1 - 259) Carbonic anhydrase 2 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00918) Carbonic anhydrasesearch Carbonic Anhydrase IIsearch PF00194: Eukaryotic-type carbonic anhydrasesearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00918) zinc ion bindingsearch lyase activitysearch protein bindingsearch metal ion bindingsearch carbonate dehydratase activitysearch cytoplasmsearch cytosolsearch apical part of cellsearch basolateral plasma membranesearch plasma membranesearch extracellular spacesearch myelin sheathsearch extracellular vesicular exosomesearch microvillussearch axonsearch membranesearch positive regulation of dipeptide transmembrane transportsearch response to estrogensearch bicarbonate transportsearch response to zinc ionsearch positive regulation of osteoclast differentiationsearch one-carbon metabolic processsearch positive regulation of synaptic transmission, GABAergicsearch regulation of anion transportsearch kidney developmentsearch regulation of chloride transportsearch angiotensin-activated signaling pathwaysearch response to steroid hormonesearch small molecule metabolic processsearch regulation of intracellular pHsearch positive regulation of bone resorptionsearch response to organic substancesearch positive regulation of cellular pH reductionsearch morphogenesis of an epitheliumsearch odontogenesis of dentin-containing toothsearch secretionsearch response to pHsearch

Chain InterPro annotation
A Alpha carbonic anhydrasesearch Carbonic anhydrase, alpha-class, conserved sitesearch Carbonic anhydrase 2search Carbonic anhydrase, alpha-classsearch