SCOPe 2.03: Domain d2wb5a2: 2wb5 A:179-495

Lineage for d2wb5a2 (2wb5 A:179-495)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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.1.8.10: alpha-D-glucuronidase/Hyaluronidase catalytic domain [82253] (3 proteins)
   Glycosyl hydrolase family 67, GH67; structurally related to GH20; contains extra C-terminal alpha-helical subdomain

6. Protein Hyaluronidase catalytic domain [141792] (1 species)

7. Species Clostridium perfringens [TaxId:1502] [141793] (7 PDB entries)
   Uniprot Q8XL08 179-495

8. Domain d2wb5a2: 2wb5 A:179-495 [206750]
   Other proteins in same PDB: d2wb5a1, d2wb5a3, d2wb5b1, d2wb5b3
   automated match to d2j62a2
   complexed with cl, na, vgb

Details for d2wb5a2

PDB Entry: 2wb5, 2.31 Å

PDB Description: glcnacstatins are nanomolar inhibitors of human o-glcnacase inducing cellular hyper-o-glcnacylation

PDB Compounds: (A:) O-GlcNAcase nagJ

SCOPe Domain Sequences for d2wb5a2:

Sequence; same for both SEQRES and ATOM records:

>d2wb5a2 c.1.8.10 (A:179-495) Hyaluronidase catalytic domain {Clostridium perfringens [TaxId: 1502]}
vsargivegfygtpwthqdrldqikfygenklntyiyapkddpyhrekwrepypesemqr
mqelinasaenkvdfvfgispgidirfdgdageedfnhlitkaeslydmgvrsfaiywdd
iqdksaakhaqvlnrfneefvkakgdvkplitvpteydtgamvsngqpraytrifaetvd
psievmwtgpgvvtneiplsdaqlisgiydrnmavwwnypvtdyfkgklalgpmhgldkg
lnqyvdfftvnpmehaelskisihtaadyswnmdnydydkawnraidmlygdlaedmkvf
anhstrmdnktwaksgr

Timeline for d2wb5a2:

• d2wb5a2 is new in SCOPe 2.03-stable
  
• d2wb5a2 appears in SCOPe 2.04
  
• d2wb5a2 appears in the current release, SCOPe 2.08