Crystal structure of human carbonic anhydrase II in complex with a benzenesulfonamide inhibitor
The structure was published by Pacchiano, F., Aggarwal, M., Avvaru, B.S., et al., Scozzafava, A., McKenna, R., and Supuran, C.T., in 2010 in a paper entitled "Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2010.
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: