HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR
The structure was published by Ramaswamy, S., Park, D.H., and Plapp, B.V., in 1999 in a paper entitled "Substitutions in the Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.07 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ALCOHOL DEHYDROGENASE. This molecule has the UniProt identifier P00327 (ADH1E_HORSE). The sample contained 374 residues which is 100% of the natural sequence. Out of 374 residues 373 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: