SCOPe 2.07: Domain d1y7va2: 1y7v A:78-431

Lineage for d1y7va2 (1y7v A:78-431)

1. Root: SCOPe 2.07

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. 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

4. Superfamily c.1.8: (Trans)glycosidases [51445] (15 families)

5. Family c.1.8.3: beta-glycanases [51487] (27 proteins)
   consist of a number of sequence families

6. 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

7. Species Human (Homo sapiens) [TaxId:9606] [89474] (23 PDB entries)

8. Domain d1y7va2: 1y7v A:78-431 [122726]
   Other proteins in same PDB: d1y7va1, d1y7vb1
   automated match to d1ogsa2
   complexed with ins, so4

Details for d1y7va2

PDB Entry: 1y7v, 2.4 Å

PDB Description: x-ray structure of human acid-beta-glucosidase covalently bound to conduritol b epoxide

PDB Compounds: (A:) glucosylceramidase

SCOPe Domain Sequences for d1y7va2:

Sequence; same for both SEQRES and ATOM records:

>d1y7va2 c.1.8.3 (A:78-431) Glucosylceramidase, catalytic domain {Human (Homo sapiens) [TaxId: 9606]}
vkgfggamtdaaalnilalsppaqnlllksyfseegigyniirvpmascdfsirtytyad
tpddfqlhnfslpeedtklkiplihralqlaqrpvsllaspwtsptwlktngavngkgsl
kgqpgdiyhqtwaryfvkfldayaehklqfwavtaenepsagllsgypfqclgftpehqr
dfiardlgptlansthhnvrllmlddqrlllphwakvvltdpeaakyvhgiavhwyldfl
apakatlgethrlfpntmlfaseacvgskfweqsvrlgswdrgmqyshsiitnllyhvvg
wtdwnlalnpeggpnwvrnfvdspiivditkdtfykqpmfyhlghfskfipegs

Timeline for d1y7va2:

• d1y7va2 first appeared in SCOP 1.73
  
• d1y7va2 appears in SCOPe 2.06
  
• d1y7va2 appears in the current release, SCOPe 2.08