![]() | Class c: Alpha and beta proteins (a/b) [51349] (141 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
![]() | Superfamily c.1.10: Aldolase [51569] (8 families) ![]() Common fold covers whole protein structure |
![]() | Family c.1.10.1: Class I aldolase [51570] (12 proteins) the catalytic lysine forms schiff-base intermediate with substrate possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels |
![]() | Protein Fructose-1,6-bisphosphate aldolase [51576] (10 species) |
![]() | Species Human (Homo sapiens), brain isozyme [TaxId:9606] [141834] (1 PDB entry) |
![]() | Domain d1xfbh1: 1xfb H:3-344 [121929] automatically matched to 1XFB A:3-344 |
PDB Entry: 1xfb (more details), 3 Å
SCOP Domain Sequences for d1xfbh1:
Sequence; same for both SEQRES and ATOM records: (download)
>d1xfbh1 c.1.10.1 (H:3-344) Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens), brain isozyme [TaxId: 9606]} hsypalsaeqkkelsdialrivapgkgilaadesvgsmakrlsqigventeenrrlyrqv lfsaddrvkkciggviffhetlyqkddngvpfvrtiqdkgivvgikvdkgvvplagtdge tttqgldglsercaqykkdgadfakwrcvlkisertpsalailenanvlaryasicqqng ivpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhvylegtllkpnmvtpghacpi kytpeeiamatvtalrrtvppavpgvtflsggqseeeasfnlnainrcplprpwaltfsy gralqasalnawrgqrdnagaateefikraevnglaaqgkye
Timeline for d1xfbh1: