SCOP 1.67: Domain d1fqaa_: 1fqa A:

Lineage for d1fqaa_ (1fqa A:)

1. Root: SCOP 1.67

2. Class c: Alpha and beta proteins (a/b) [51349] (130 folds)

3. Fold c.94: Periplasmic binding protein-like II [53849] (1 superfamily)
   consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication
   mixed beta-sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest

4. Superfamily c.94.1: Periplasmic binding protein-like II [53850] (2 families)
   Similar in architecture to the superfamily I but partly differs in topology

5. Family c.94.1.1: Phosphate binding protein-like [53851] (26 proteins)

6. Protein D-maltodextrin-binding protein, MBP [53862] (4 species)
   contains a few additional helices in the C-terminal extension; homologous to thiaminase I

7. Species Escherichia coli [TaxId:562] [53863] (35 PDB entries)

8. Domain d1fqaa_: 1fqa A: [59984]
   complexed with glc, glo

Details for d1fqaa_

PDB Entry: 1fqa, 1.9 Å

PDB Description: structure of maltotetraitol bound to open-form maltodextrin binding protein in p2(1)crystal form

SCOP Domain Sequences for d1fqaa_:

Sequence; same for both SEQRES and ATOM records:

>d1fqaa_ c.94.1.1 (A:) D-maltodextrin-binding protein, MBP {Escherichia coli}
aieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk

Timeline for d1fqaa_:

• d1fqaa_ first appeared in SCOP 1.57
  
• d1fqaa_ appears in SCOP 1.65
  
• d1fqaa_ appears in SCOP 1.69
  
• d1fqaa_ appears in the current release, SCOPe 2.08, called d1fqaa1