![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (34 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] (9 families) ![]() Common fold covers whole protein structure |
![]() | Family c.1.10.1: Class I aldolase [51570] (13 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] (11 species) |
![]() | Species Human (Homo sapiens) [TaxId:9606] [254964] (6 PDB entries) |
![]() | Domain d1xdmz_: 1xdm Z: [121887] automated match to d1fdja_ complexed with so4 |
PDB Entry: 1xdm (more details), 3 Å
SCOPe Domain Sequences for d1xdmz_:
Sequence, based on SEQRES records: (download)
>d1xdmz_ c.1.10.1 (Z:) Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens) [TaxId: 9606]} paltqeqkkelseiaqsivangkgilaadesvgtmgnrlqrikventeenrrqfreilfs vdssinqsiggvilfhetlyqkdsqgklfrnilkekgivvgikldqggaplagtnketti qgldglsercaqykkdgvdfgkwrpvlriadqcpsslaiqenanalaryasicqqnglvp ivepevipdgdhdlehcqyvtekvlaavykalndhhvylegtllkpnmvtaghactkkyt peqvamatvtalhrtvpaavpgicflsggmseedatlnlnainlcplpkpwklsfsygra lqasalaawggkaankeatqeafmkramancqaakgqy
>d1xdmz_ c.1.10.1 (Z:) Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens) [TaxId: 9606]} paltqeqkkelseiaqsivangkgilaadesvgtmgnrlqrikventeenrrqfreilfs vdssinqsiggvilfhetlyqkdsqgklfrnilkekgivvgiklddglsercaqykkdgv dfgkwrsslaiqenanalaryasicqqnglvpivepedlehcqyvtekvlaavykalndh hvylegtllkpnmvtytpeqvamatvtalhrtvpaavpgicflsggmseedatlnlnain lcplpkpwklsfsygralqasalaawggkaankeatqeafmkramancqaakgqy
Timeline for d1xdmz_: