2aat Summary



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)search. 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A ASPARTATE AMINOTRANSFERASE P00509 (1-396) (AAT_ECOLI)search Escherichia coli K-12search 98% 396 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00509 (1 - 396) ASPARTATE AMINOTRANSFERASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00509) AAT-likesearch Aspartate Aminotransferase, domain 1search, Type I PLP-dependent aspartate aminotransferase-like (Major domain)search PF00155: Aminotransferase class I and IIsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P00509) cytoplasmsearch cytosolsearch L-phenylalanine biosynthetic processsearch cellular amino acid metabolic processsearch L-phenylalanine biosynthetic process from chorismate via phenylpyruvatesearch biosynthetic processsearch L-aspartate:2-oxoglutarate aminotransferase activitysearch pyridoxal phosphate bindingsearch catalytic activitysearch transaminase activitysearch transferase activitysearch identical protein bindingsearch L-phenylalanine:2-oxoglutarate aminotransferase activitysearch L-tyrosine:2-oxoglutarate aminotransferase activitysearch

Chain InterPro annotation
A Aspartate/other aminotransferasesearch Aminotransferase, class I/classIIsearch Pyridoxal phosphate-dependent transferase, major region, subdomain 1search Pyridoxal phosphate-dependent transferasesearch