SCOPe 2.07: Domain d2qmja2: 2qmj A:270-649

Lineage for d2qmja2 (2qmj A:270-649)

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.1.8.13: 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 d2qmja2: 2qmj A:270-649 [304428]
   Other proteins in same PDB: d2qmja1, d2qmja3, d2qmja4, d2qmja5
   automated match to d2qlya2
   complexed with acr, gol, nag, so4

Details for d2qmja2

PDB Entry: 2qmj, 1.9 Å

PDB Description: crystral structure of the n-terminal subunit of human maltase- glucoamylase in complex with acarbose

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

SCOPe Domain Sequences for d2qmja2:

Sequence; same for both SEQRES and ATOM records:

>d2qmja2 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 d2qmja2:

• d2qmja2 first appeared in SCOPe 2.06
  
• d2qmja2 appears in the current release, SCOPe 2.08