SCOP 1.75: Domain d1y7va1: 1y7v A:1-77,A:432-497

Lineage for d1y7va1 (1y7v A:1-77,A:432-497)

1. Root: SCOP 1.75

2. Class b: All beta proteins [48724] (174 folds)

3. Fold b.71: Glycosyl hydrolase domain [51010] (1 superfamily)
   folded sheet; greek-key

4. Superfamily b.71.1: Glycosyl hydrolase domain [51011] (5 families)
   this domain is C-terminal to the catalytic beta/alpha barrel domain

5. Family b.71.1.2: Composite domain of glycosyl hydrolase families 5, 30, 39 and 51 [89388] (4 proteins)
   interrupted by the catalytic domain; the C-terminal core is similar to the alpha-amylase domain

6. Protein Glucosylceramidase [89389] (1 species)
   glycosyl hydrolase family 30; the N-terminal extension wraps around the C-terminal core

7. Species Human (Homo sapiens) [TaxId:9606] [89390] (11 PDB entries)

8. Domain d1y7va1: 1y7v A:1-77,A:432-497 [122725]
   Other proteins in same PDB: d1y7va2, d1y7vb2
   automatically matched to d1ogsa1
   complexed with ins, nag, so4; mutant

Details for d1y7va1

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

SCOP Domain Sequences for d1y7va1:

Sequence; same for both SEQRES and ATOM records:

>d1y7va1 b.71.1.2 (A:1-77,A:432-497) Glucosylceramidase {Human (Homo sapiens) [TaxId: 9606]}
arpcipksfgyssvvcvcnatycdsfdpptfpalgtfsryestrsgrrmelsmgpiqanh
tgtgllltlqpeqkfqkXqrvglvasqkndldavalmhpdgsavvvvlnrsskdvpltik
dpavgfletispgysihtylwhrq

Timeline for d1y7va1:

• d1y7va1 first appeared in SCOP 1.73
  
• d1y7va1 appears in SCOPe 2.01
  
• d1y7va1 appears in the current release, SCOPe 2.08