MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT
The structure was published by Collyer, C.A., Henrick, K., and Blow, D.M., in 1990 in a paper entitled "Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1991.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of D-XYLOSE 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 homotetramers.
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: