X-RAY ANALYSIS OF D-XYLOSE ISOMERASE AT 1.9 ANGSTROMS: NATIVE ENZYME IN COMPLEX WITH SUBSTRATE AND WITH A MECHANISM-DESIGNED INACTIVATOR
The structure was published by Carrell, H.L., Glusker, J.P., Burger, V., Manfre, F., Tritsch, D., and Biellmann, J.F., in 1989 in a paper entitled "X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1990.
The experimental data on which the structure is based was not 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 387 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: