Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APK_2nde3gqyA4 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
APK_1ste3gqyA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
APK_Ce3gqyA3 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)
BPK_2nde3gqyB1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
BPK_1ste3gqyB2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
BPK_Ce3gqyB3 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)
CPK_2nde3gqyC1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
CPK_1ste3gqyC3 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
CPK_Ce3gqyC2 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)
DPK_2nde3gqyD4 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
DPK_1ste3gqyD2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
DPK_Ce3gqyD1 A: a/b three-layered sandwichesX: PK C-terminal domain-like (From Topology)H: PK C-terminal domain-like (From Topology)T: PK C-terminal domain-likeF: PK_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF02887Pyruvate kinase, alpha/beta domain (PK_C)Pyruvate kinase, alpha/beta domainPyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, ...Pyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, 3,4]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain (represented in this entry). This domain is at the C-terminal of pyruvate kinases and contains the FBP (fructose 1,6-bisphosphate) binding site [2,4,5].
Domain
A, B, C, D
PF00224Pyruvate kinase, barrel domain (PK)Pyruvate kinase, barrel domainThis is the barrel domain of pyruvate kinases. This domain represents the beta/alpha barrel and the small beta-barrel domain inserted within it. The active site is found in a cleft between the two domains [1,2,3,4].Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
Pyruvate kinase isozymes M1/M2