SCOPe 2.07: Domain d3sesc1: 3ses C:2-359

Lineage for d3sesc1 (3ses C: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 protein domains)

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] (68 PDB entries)
   Uniprot P02928

8. Domain d3sesc1: 3ses C:2-359 [216367]
   Other proteins in same PDB: d3sesa2, d3sesc2
   automated match to d1a7lc_
   complexed with cl, cu, mal

Details for d3sesc1

PDB Entry: 3ses, 1.9 Å

PDB Description: Cu-mediated Dimer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization

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

SCOPe Domain Sequences for d3sesc1:

Sequence; same for both SEQRES and ATOM records:

>d3sesc1 c.94.1.1 (C:2-359) D-maltodextrin-binding protein, MBP {Escherichia coli [TaxId: 562]}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaehafnhgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvd

Timeline for d3sesc1:

• d3sesc1 first appeared in SCOPe 2.03, called d3sesc_
  
• d3sesc1 appears in SCOPe 2.06