Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
The structure was published by Fisher, S.Z., Tu, C.K., Bhatt, D., et al., Agbandje-McKenna, M., McKenna, R., and Silverman, D.N., in 2007 in a paper entitled "Speeding Up Proton Transfer in a Fast Enzyme: Kinetic and Crystallographic Studies on the Effect of Hydrophobic Amino Acid Substitutions in the Active Site of Human Carbonic Anhydrase II." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.15 Å and deposited in 2006.
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 257 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: