The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase
The structure was published by Hubbard, P.A., Liang, X., Schulz, H., and Kim, J.J., in 2003 in a paper entitled "The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of 2,4-dienoyl-CoA reductase. This molecule has the UniProt identifier P42593 (FADH_ECOLI). The sample contained 671 residues which is 100% of the natural sequence. Out of 671 residues 671 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 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: