X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
The structure was published by Lavie, A., Allen, K.N., Petsko, G.A., and Ringe, D., in 1994 in a paper entitled "X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.96 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of 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: