STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
The structure was published by Nair, S.K. and Christianson, D.W., in 1993 in a paper entitled "Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1992.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of CARBONIC ANHYDRASE II. 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 255 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: