2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI
The structure was published by Smith, D.L., Almo, S.C., Toney, M.D., and Ringe, D., in 1989 in a paper entitled "2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1989.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of ASPARTATE AMINOTRANSFERASE. This molecule has the UniProt identifier P00509 (AAT_ECOLI). The sample contained 396 residues which is 100% of the natural sequence. Out of 396 residues 396 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: