ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS
The structure was published by Mrabet, N.T., Van den Broeck, A., Van den brande, I., et al., Lasters, I., Demaeyer, M., and Wodak, S.J., in 1992 in a paper entitled "Arginine residues as stabilizing elements in proteins." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 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: