SCOPe 2.01: Domain d1mdp2_: 1mdp 2:

Lineage for d1mdp2_ (1mdp 2:)

1. Root: SCOPe 2.01

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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] (4 families)
   Similar in architecture to the superfamily I but partly differs in topology

5. Family c.94.1.1: Phosphate binding protein-like [53851] (41 proteins)

6. Protein D-maltodextrin-binding protein, MBP [53862] (5 species)
   contains a few additional helices in the C-terminal extension; homologous to thiaminase I

7. Species Escherichia coli [TaxId:562] [53863] (47 PDB entries)
   Uniprot P02928

8. Domain d1mdp2_: 1mdp 2: [35785]
   complexed with mal; mutant

Details for d1mdp2_

PDB Entry: 1mdp, 2.3 Å

PDB Description: refined structures of two insertion(slash)deletion mutants probe function of the maltodextrin binding protein

PDB Compounds: (2:) maltodextrin binding protein

SCOPe Domain Sequences for d1mdp2_:

Sequence; same for both SEQRES and ATOM records:

>d1mdp2_ c.94.1.1 (2:) D-maltodextrin-binding protein, MBP {Escherichia coli [TaxId: 562]}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipdpgksalmfnlqepyftwpliaadggyafkyengkydikdvgvdnag
akagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnygvtvl
ptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgavalksy
eeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkdaqtr
itk

Timeline for d1mdp2_:

• d1mdp2_ first appeared (with stable ids) in SCOP 1.55
  
• d1mdp2_ appears in SCOP 1.75
  
• d1mdp2_ appears in SCOPe 2.02
  
• d1mdp2_ appears in the current release, SCOPe 2.08