SCOPe 2.06: Domain d2qlya2: 2qly A:270-649

Lineage for d2qlya2 (2qly A:270-649)

1. Root: SCOPe 2.06

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.1.8.13: Glycosyl hydrolase family 31 catalytic domain [117372] (5 proteins)
   Pfam PF01055

6. Protein N-terminal subunit of Maltase-glucoamylase (NtMGAM), catalytic domain [310750] (1 species)

7. Species Human (Homo sapiens) [TaxId:9606] [311005] (3 PDB entries)

8. Domain d2qlya2: 2qly A:270-649 [304423]
   Other proteins in same PDB: d2qlya1, d2qlya3, d2qlya4, d2qlya5
   complexed with gol, nag

Details for d2qlya2

PDB Entry: 2qly, 2 Å

PDB Description: crystral structure of the n-terminal subunit of human maltase- glucoamylase

PDB Compounds: (A:) Maltase-glucoamylase, intestinal

SCOPe Domain Sequences for d2qlya2:

Sequence; same for both SEQRES and ATOM records:

>d2qlya2 c.1.8.13 (A:270-649) N-terminal subunit of Maltase-glucoamylase (NtMGAM), catalytic domain {Human (Homo sapiens) [TaxId: 9606]}
peqvvqeyleligrpalpsywalgfhlsryeygtldnmrevvernraaqlpydvqhadid
ymderrdftydsvdfkgfpefvnelhnngqklviivdpaisnnsssskpygpydrgsdmk
iwvnssdgvtpligevwpgqtvfpdytnpncavwwtkefelfhnqvefdgiwidmnevsn
fvdgsvsgcstnnlnnppftprildgylfcktlcmdavqhwgkqydihnlygysmavata
eaaktvfpnkrsfiltrstfagsgkfaahwlgdntatwddlrwsipgvlefnlfgipmvg
pdicgfaldtpeelcrrwmqlgafypfsrnhngqgykdqdpasfgadslllnssrhylni
rytllpylytlffrahsrgd

Timeline for d2qlya2:

• d2qlya2 is new in SCOPe 2.06-stable
  
• d2qlya2 appears in SCOPe 2.07
  
• d2qlya2 appears in the current release, SCOPe 2.08