Navigation Tabs
CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS External Resource: Annotation Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2 Family Precorrin-8X methylmutase CbiC/CobH 8020532 4003365 SCOP2 (2022-06-29) A SCOP2 Superfamily Precorrin-8X methylmutase CbiC/CobH 8032912 3000708 SCOP2 (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A CbiC e1f2vA1 A: a/b three-layered sandwiches X: Flavodoxin-like H: Precorrin-8X methylmutase CbiC/CobH (From Topology) T: Precorrin-8X methylmutase CbiC/CobH F: CbiC ECOD (1.6)
Chains Polymer Molecular Function Biological Process Cellular Component PRECORRIN-8X METHYLMUTASE -
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage Chains Enzyme Name Description Catalytic Residues precorrin-8X methylmutase
M-CSA #193 Precorrin-8x methyl mutase (CobH) catalyses the migration of a methyl group attached to C-11 of the substrate, precorrin-8x, to the adjacent C-12 to give the product hydrogenobyrinic acid (HBA).This is a step in the aerobic biosynthesis of the corrin macrocycle of vitamin B12.
View More
At least 2 residues must be present to support Structure Motif searching.