1PKM

THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyPyruvate kinase beta-barrel domain 8030172 4002474 SCOP2 (2022-06-29)
ASCOP2 FamilyPyruvate kinase 8031259 4003255 SCOP2 (2022-06-29)
ASCOP2 FamilyPK C-terminal domain-like 8032023 4000500 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyPK beta-barrel domain-like 8042551 3001296 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyPhosphoenolpyruvate/pyruvate domain 8043637 3000510 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyPK C-terminal domain-like 8044401 3000442 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APK_2nde1pkmA4 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: PK beta-barrel domain-likeF: PK_2ndECOD (1.6)
APK_1ste1pkmA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PK_1stECOD (1.6)
APK_Ce1pkmA2 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

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.1380.20 Alpha Beta 3-Layer(aba) Sandwich Pyruvate Kinase Chain: A, domain 1CATH (4.3.0)
A3.20.20.60 Alpha Beta Alpha-Beta Barrel TIM Barrel Phosphoenolpyruvate-binding domainsCATH (4.3.0)
A2.40.33.10 Mainly Beta Beta Barrel M1 Pyruvate Kinase Domain 3CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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
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
M1 PYRUVATE KINASE