1FP1 | pdb_00001fp1

CRYSTAL STRUCTURE ANALYSIS OF CHALCONE O-METHYLTRANSFERASE


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth D]SCOP2 FamilyPlant O-methyltransferase-like 8003408 4000240 SCOP2 (2022-06-29)
A [auth D]SCOP2 SuperfamilyS-adenosyl-L-methionine-dependent methyltransferases 8003409 3000118 SCOP2 (2022-06-29)
A [auth D]SCOP2 SuperfamilyWinged helix DNA-binding domain 8003411 3000034 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth D]Dimerisatione1fp1D1 A: alpha arraysX: HTHH: HTHT: wingedF: DimerisationECOD (1.6)
A [auth D]Methyltransf_11_4e1fp1D2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Methyltransf_11_4ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth D]PF08100Plant O-methyltransferase dimerisation domain (Dimerisation)Plant O-methyltransferase dimerisation domainThis domain is found at the N-terminus of plant O-methyltransferases involved in phenylpropanoid metabolism, including caffeic acid O-methyltransferase (COMT), isoflavone O-methyltransferase (IOMT), and chalcone O-methyltransferase (ChOMT). It media ...This domain is found at the N-terminus of plant O-methyltransferases involved in phenylpropanoid metabolism, including caffeic acid O-methyltransferase (COMT), isoflavone O-methyltransferase (IOMT), and chalcone O-methyltransferase (ChOMT). It mediates dimerisation of these enzymes, which is critical for their activity [1-4]. The dimerisation domain forms the central core of the homodimer, with the SAM-binding domains located peripherally [1,3,4]. Dimerisation buries ~30% of the total surface area of the dimer [3]. The domain also contributes to forming the back wall of the substrate binding cavity of the partner monomer [2-4]. Structurally, the dimerisation domain consists primarily of alpha-helices [1-4]. Crystal structures reveal the domain is relatively rigid compared to the more mobile SAM-binding domain, which undergoes conformational changes upon substrate binding [4].
Domain
A [auth D]PF00891O-methyltransferase domain (Methyltransf_2)O-methyltransferase domainThis family includes a range of O-methyltransferases. These enzymes utilise S-adenosyl methionine. Domain