1hti Summary

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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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A TRIOSEPHOSPHATE ISOMERASE P60174 (39-286) (TPIS_HUMAN)search Homo sapienssearch < 90% 248 100%
B TRIOSEPHOSPHATE ISOMERASE P60174 (39-286) (TPIS_HUMAN)search Homo sapienssearch < 90% 248 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P60174 (39 - 286) TRIOSEPHOSPHATE ISOMERASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Triosephosphate isomerase (TIM)search Aldolase class Isearch Triosephosphate isomerasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P60174) triose-phosphate isomerase activitysearch catalytic activitysearch metabolic processsearch glycolytic processsearch

Chain InterPro annotation
A, B Triosephosphate isomerasesearch Aldolase-type TIM barrelsearch Triosephosphate isomerase, active sitesearch Triosephosphate isomerase, bacterial/eukaryoticsearch