STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP
The structure was published by Wouters, J., Oudjama, Y., Barkley, S.J., et al., Stalon, V., Droogmans, L., and Poulter, C.D., in 2003 in a paper entitled "Catalytic Mechanism of Escherichia coli Isopentenyl Diphosphate Isomerase Involves Cys-67, Glu-116, and Tyr-104 as Suggested by Crystal Structures of Complexes with Transition State Analogues and Irreversible Inhibitors" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.96 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE.
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):
This entry contains 1 unique UniProt protein: