HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A
The structure was published by Parris, K.D., Lin, L., Tam, A., et al., Fritz, C.C., Seehra, J., and Somers, W.S., in 2000 in a paper entitled "Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2000.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of HOLO-(ACYL CARRIER PROTEIN) SYNTHASE. This molecule has the UniProt identifier P96618 (ACPS_BACSU). The sample contained 121 residues which is 100% of the natural sequence. Out of 121 residues 116 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 homotrimers.
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: