Room temperature neutron structure of D-Xylose Isomerase in complex with two Cd2+ cations and d12-D-alpha-glucose in the ring form (refined jointly with X-ray structure 3KBM)
The structure was published by Kovalevsky, A.Y., Hanson, L., Fisher, S.Z., et al., Katz, A.K., Glusker, J.P., and Langan, P., in 2010 in a paper entitled "Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: a joint x-ray and neutron diffraction study." (abstract).
The structure was determined using a combination of experimental techniques (Neutron diffraction and X-ray diffraction) at a resolution of 2.0 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Xylose isomerase. This molecule has the UniProt identifier P24300 (XYLA_STRRU). The sample contained 388 residues which is 100% of the natural sequence. Out of 388 residues 388 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 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: