2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5
The structure was published by Engel, C.K., Mathieu, M., Zeelen, J.P., Hiltunen, J.K., and Wierenga, R.K., in 1996 in a paper entitled "Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1996.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of 2-ENOYL-COA HYDRATASE.
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 homohexamers.
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: