1MSS

LARGE SCALE STRUCTURAL REARRANGEMENTS OF THE FRONT LOOPS IN MONOMERISED TRIOSEPHOSPHATE ISOMERASE, AS DEDUCED FROM THE COMPARISON OF THE STRUCTURAL PROPERTIES OF MONOTIM AND ITS POINT MUTATION VARIANT MONOSS


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyTriosephosphate isomerase (TIM) 8040644 3000190 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyTriosephosphate isomerase (TIM) 8040644 3000190 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BTIMe1mssB1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: TIMECOD (1.6)
ATIMe1mssA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: TIMECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.20.20.70 Alpha Beta Alpha-Beta Barrel TIM Barrel Aldolase class ICATH (4.3.0)
A3.20.20.70 Alpha Beta Alpha-Beta Barrel TIM Barrel Aldolase class ICATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00121Triosephosphate isomerase (TIM)Triosephosphate isomeraseTriosephosphate isomerase (EC:5.3.1.1) (TIM) [1] is the glycolytic enzyme that catalyses the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is ess ...Triosephosphate isomerase (EC:5.3.1.1) (TIM) [1] is the glycolytic enzyme that catalyses the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism [2,3]. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure [4]. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder [5].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
TRIOSEPHOSPHATE ISOMERASE