![]() | Class c: Alpha and beta proteins (a/b) [51349] (147 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.1.8: (Trans)glycosidases [51445] (14 families) ![]() |
![]() | Family c.1.8.3: beta-glycanases [51487] (26 proteins) consist of a number of sequence families |
![]() | Protein Glucosylceramidase, catalytic domain [89473] (1 species) acid-beta-glucosidase; glycosyl hydrolase family 30; contains additional beta-domain similar to one found in alpha amylases |
![]() | Species Human (Homo sapiens) [TaxId:9606] [89474] (11 PDB entries) |
![]() | Domain d2v3ea2: 2v3e A:78-431 [152450] Other proteins in same PDB: d2v3ea1, d2v3eb1 automatically matched to d1ogsa2 complexed with bma, fuc, nag, nnd, po4 |
PDB Entry: 2v3e (more details), 2 Å
SCOP Domain Sequences for d2v3ea2:
Sequence; same for both SEQRES and ATOM records: (download)
>d2v3ea2 c.1.8.3 (A:78-431) Glucosylceramidase, catalytic domain {Human (Homo sapiens) [TaxId: 9606]} vkgfggamtdaaalnilalsppaqnlllksyfseegigyniirvpmascdfsirtytyad tpddfqlhnfslpeedtklkiplihralqlaqrpvsllaspwtsptwlktngavngkgsl kgqpgdiyhqtwaryfvkfldayaehklqfwavtaenepsagllsgypfqclgftpehqr dfiardlgptlansthhnvrllmlddqrlllphwakvvltdpeaakyvhgiavhwyldfl apakatlgethrlfpntmlfaseacvgskfweqsvrlgswdrgmqyshsiitnllyhvvg wtdwnlalnpeggpnwvrnfvdspiivditkdtfykqpmfyhlghfskfipegs
Timeline for d2v3ea2: