Apo-human carbonic anhydrase II revisited: Implications of the loss of a metal in protein structure, stability and solvent network
The structure was published by Avvaru, B.S., Busby, S.A., Chalmers, M.J., et al., Agbandje-McKenna, M., Silverman, D.N., and McKenna, R., in 2009 in a paper entitled "Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of a Metal in Protein Structure, Stability, and Solvent Network ." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.26 Å and deposited in 2009.
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 259 residues which is 100% of the natural sequence. Out of 259 residues 256 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: