Crystal structure of SeMet-substituted N-terminal truncated human B12-chaperone CblD (108-296)
Structure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN Reductases.
K-B pair of biomorph mirrors for vertical and horizontal focusing
Methylmalonic aciduria and homocystinuria type D protein, mitochondrial
GH(MSE)SSERHEFV(MSE)AQYVNEFQGNDAPVEQEINSAETYFESARVECAIQTCPELLRKDFESLFPEVANGKL (MSE)ILTVTQKTKND(MSE)TVWSEEVEIEREVLLEKFINGAKEICYALRAEGYWADFIDPSSGLAFFGPYTNNTLFET DERYRHLGFSVDDLGCCKVIRHSLWGTHVVVGSIFTNATPDSHI(MSE)KKLSGN
GHMSSERHEFVMAQYVNEFQGNDAPVEQEINSAETYFESARVECAIQTCPELLRKDFESLFPEVANGKLMILTVTQKTKN DMTVWSEEVEIEREVLLEKFINGAKEICYALRAEGYWADFIDPSSGLAFFGPYTNNTLFETDERYRHLGFSVDDLGCCKV IRHSLWGTHVVVGSIFTNATPDSHIMKKLSGN
MMADHC, C2orf25, CL25022, HSPC161, My011
HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Vitamin B12, Nitro-FMN-reductase, CHAPERONE
SSERHEFVMAQYVNEFQGNDAPVEQEINSAETYFESARVECAIQTCPELLRKDFESLFPEVANGKLMILTVTQKTKNDMT VWSEEVEIEREVLLEKFINGAKEICYALRAEGYWADFIDPSSGLAFFGPYTNNTLFETDERYRHLGFSVDDLGCCKVIRH SLWGTHVVVGSIFTNATPDSHIMKKLSGN