SCOPe 2.07: Domain d3seva1: 3sev A:2-359

Lineage for d3seva1 (3sev A:2-359)

1. Root: SCOPe 2.07

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (45 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] (69 PDB entries)
   Uniprot P02928

8. Domain d3seva1: 3sev A:2-359 [249417]
   Other proteins in same PDB: d3seva2, d3sevc2, d3seve2
   automated match to d3pgfa_
   complexed with cl, mal, zn

Details for d3seva1

PDB Entry: 3sev, 3.05 Å

PDB Description: zn-mediated trimer of maltose-binding protein e310h/k314h by synthetic symmetrization

PDB Compounds: (A:) Maltose-binding periplasmic protein

SCOPe Domain Sequences for d3seva1:

Sequence; same for both SEQRES and ATOM records:

>d3seva1 c.94.1.1 (A:2-359) D-maltodextrin-binding protein, MBP {Escherichia coli [TaxId: 562]}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyehelahdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvd

Timeline for d3seva1:

• d3seva1 first appeared in SCOPe 2.04, called d3seva_
  
• d3seva1 appears in SCOPe 2.06
  
• d3seva1 appears in the current release, SCOPe 2.08