MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE
The structure was published by Carrell, H.L., Hoier, H., and Glusker, J.P., in 1994 in a paper entitled "Modes of binding substrates and their analogues to the enzyme D-xylose isomerase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of D-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 385 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: