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). 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):
This entry contains 1 unique UniProt protein: