![]() | 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), liver isozyme [TaxId:9606] [51578] (3 PDB entries) |
![]() | Domain d1xdmz1: 1xdm Z:6-342 [121887] automatically matched to 1XDL A:6-343 complexed with so4; mutant |
PDB Entry: 1xdm (more details), 3 Å
SCOP Domain Sequences for d1xdmz1:
Sequence, based on SEQRES records: (download)
>d1xdmz1 c.1.10.1 (Z:6-342) Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens), liver isozyme [TaxId: 9606]} altqeqkkelseiaqsivangkgilaadesvgtmgnrlqrikventeenrrqfreilfsv dssinqsiggvilfhetlyqkdsqgklfrnilkekgivvgikldqggaplagtnkettiq gldglsercaqykkdgvdfgkwrpvlriadqcpsslaiqenanalaryasicqqnglvpi vepevipdgdhdlehcqyvtekvlaavykalndhhvylegtllkpnmvtaghactkkytp eqvamatvtalhrtvpaavpgicflsggmseedatlnlnainlcplpkpwklsfsygral qasalaawggkaankeatqeafmkramancqaakgqy
>d1xdmz1 c.1.10.1 (Z:6-342) Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens), liver isozyme [TaxId: 9606]} altqeqkkelseiaqsivangkgilaadesvgtmgnrlqrikventeenrrqfreilfsv dssinqsiggvilfhetlyqkdsqgklfrnilkekgivvgiklddglsercaqykkdgvd fgkwrsslaiqenanalaryasicqqnglvpivepedlehcqyvtekvlaavykalndhh vylegtllkpnmvtytpeqvamatvtalhrtvpaavpgicflsggmseedatlnlnainl cplpkpwklsfsygralqasalaawggkaankeatqeafmkramancqaakgqy
Timeline for d1xdmz1: