CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME
The structure was published by Mande, S.C., Mainfroid, V., Kalk, K.H., Goraj, K., Martial, J.A., and Hol, W.G., in 1994 in a paper entitled "Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 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 TRIOSEPHOSPHATE 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 homodimers.
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: