HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.184.108.40.206) MUTANT WITH ALA 65 REPLACED BY SER (A65S)
The structure was published by Scolnick, L.R. and Christianson, D.W., in 1996 in a paper entitled "X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1996.
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 258 residues which is 99% of the natural sequence. Out of 258 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: