TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE
The structure was published by Xiang, S., Short, S.A., Wolfenden, R., and Carter Jr., C.W., in 1995 in a paper entitled "Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1995.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of CYTIDINE DEAMINASE. This molecule has the UniProt identifier P0ABF6 (CDD_ECOLI). The sample contained 294 residues which is 100% of the natural sequence. Out of 294 residues 294 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 most likely forms homodimers.
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: