Lineage for d2nsxb2 (2nsx B:78-431)

  1. Root: SCOPe 2.08
  2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 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
  4. Superfamily c.1.8: (Trans)glycosidases [51445] (15 families) (S)
  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 d2nsxb2: 2nsx B:78-431 [138555]
    Other proteins in same PDB: d2nsxa1, d2nsxb1, d2nsxc1, d2nsxd1
    automated match to d1ogsa2
    complexed with gol, ifm, nag, so4

Details for d2nsxb2

PDB Entry: 2nsx (more details), 2.11 Å

PDB Description: structure of acid-beta-glucosidase with pharmacological chaperone provides insight into gaucher disease
PDB Compounds: (B:) glucosylceramidase

SCOPe Domain Sequences for d2nsxb2:

Sequence; same for both SEQRES and ATOM records: (download)

>d2nsxb2 c.1.8.3 (B:78-431) Glucosylceramidase, catalytic domain {Human (Homo sapiens) [TaxId: 9606]}
vkgfggamtdaaalnilalsppaqnlllksyfseegigyniirvpmascdfsirtytyad
tpddfqlhnfslpeedtklkiplihralqlaqrpvsllaspwtsptwlktngavngkgsl
kgqpgdiyhqtwaryfvkfldayaehklqfwavtaenepsagllsgypfqclgftpehqr
dfiardlgptlansthhnvrllmlddqrlllphwakvvltdpeaakyvhgiavhwyldfl
apakatlgethrlfpntmlfaseacvgskfweqsvrlgswdrgmqyshsiitnllyhvvg
wtdwnlalnpeggpnwvrnfvdspiivditkdtfykqpmfyhlghfskfipegs

SCOPe Domain Coordinates for d2nsxb2 are not available.

Timeline for d2nsxb2:

Domains from same chain:
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d2nsxb1
Domains from other chains:
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d2nsxa1, d2nsxa2, d2nsxc1, d2nsxc2, d2nsxd1, d2nsxd2