The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
The structure was published by Snyder, P.W., Mecinovic, J., Moustakas, D.T., et al., Heroux, A., Sherman, W., and Whitesides, G.M., in 2011 in a paper entitled "Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2011.
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 258 residues which is 99% of the natural sequence. Out of 258 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: