THE ESCHERICHIA COLI MALONYL-COA:ACYL CARRIER PROTEIN TRANSACYLASE AT 1.5-ANGSTROMS RESOLUTION. CRYSTAL STRUCTURE OF A FATTY ACID SYNTHASE COMPONENT
The structure was published by Serre, L., Verbree, E.C., Dauter, Z., Stuitje, A.R., and Derewenda, Z.S., in 1995 in a paper entitled "The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 1995.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of MALONYL-COENZYME A ACYL CARRIER PROTEIN TRANSACYLASE. This molecule has the UniProt identifier P0AAI9 (FABD_ECOLI). The sample contained 309 residues which is 100% of the natural sequence. Out of 309 residues 305 were observed and are deposited in the PDB.
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: