Entry Database : PDB / ID : 2jk2 Structure visualization Downloads & linksTitle STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. CRYSTAL STRUCTURE OF THE WILD TYPE ENZYME. ComponentsTRIOSEPHOSPHATE ISOMERASE Details Keywords ISOMERASE / ALTERNATIVE SPLICING / FATTY ACID BIOSYNTHESIS / LIPID SYNTHESIS / DISEASE MUTATION / PENTOSE SHUNT / PHOSPHOPROTEIN / GLUCONEOGENESIS / GLYCOLYSIS / ACETYLATION / POLYMORPHISMFunction / homology Function and homology informationFunction Domain/homology Component
methylglyoxal biosynthetic process / methylglyoxal synthase / methylglyoxal synthase activity / triose-phosphate isomerase / triose-phosphate isomerase activity / Gluconeogenesis / glyceraldehyde-3-phosphate biosynthetic process / canonical glycolysis / glycerol catabolic process / Glycolysis ... methylglyoxal biosynthetic process / methylglyoxal synthase / methylglyoxal synthase activity / triose-phosphate isomerase / triose-phosphate isomerase activity / Gluconeogenesis / glyceraldehyde-3-phosphate biosynthetic process / canonical glycolysis / glycerol catabolic process / Glycolysis / gluconeogenesis / glycolytic process / ubiquitin protein ligase binding / protein homodimerization activity / extracellular space / extracellular exosome / nucleus / cytosol Similarity search - Function Triosephosphate isomerase, bacterial/eukaryotic / Triosephosphate isomerase, active site / Triosephosphate isomerase active site. / Triosephosphate isomerase / Triosephosphate isomerase superfamily / Triosephosphate isomerase / Triosephosphate isomerase (TIM) family profile. / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel ... Triosephosphate isomerase, bacterial/eukaryotic / Triosephosphate isomerase, active site / Triosephosphate isomerase active site. / Triosephosphate isomerase / Triosephosphate isomerase superfamily / Triosephosphate isomerase / Triosephosphate isomerase (TIM) family profile. / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.7 Å DetailsAuthors Rodriguez-Almazan, C. / Arreola-Alemon, R. / Rodriguez-Larrea, D. / Aguirre-Lopez, B. / De Gomez-Puyou, M.T. / Perez-Montfort, R. / Costas, M. / Gomez-Puyou, A. / Torres-Larios, A. CitationJournal : J.Biol.Chem. / Year : 2008Title : Structural Basis of Human Triosephosphate Isomerase Deficiency: Mutation E104D is Related to Alterations of a Conserved Water Network at the Dimer Interface.Authors : Rodriguez-Almazan, C. / Arreola, R. / Rodriguez-Larrea, D. / Aguirre-Lopez, B. / De Gomez-Puyou, M.T. / Perez-Montfort, R. / Costas, M. / Gomez-Puyou, A. / Torres-Larios, A. History Deposition Jun 22, 2008 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jul 1, 2008 Provider : repository / Type : Initial releaseRevision 1.1 May 7, 2011 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Show all Show less Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA", "BA" IN EACH CHAIN ON SHEET RECORDS ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA", "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.