SCOPe 2.02: Domain d1laxa_: 1lax A:

Lineage for d1laxa_ (1lax A:)

1. Root: SCOPe 2.02

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 d1laxa_: 1lax A: [84576]
   mutant

Details for d1laxa_

PDB Entry: 1lax, 1.85 Å

PDB Description: crystal structure of male31, a defective folding mutant of maltose- binding protein

PDB Compounds: (A:) maltose-binding protein mutant male31

SCOPe Domain Sequences for d1laxa_:

Sequence; same for both SEQRES and ATOM records:

>d1laxa_ c.94.1.1 (A:) D-maltodextrin-binding protein, MBP {Escherichia coli [TaxId: 562]}
kieegklviwingdkgynglaevgkkfekdtdpkvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtrit

Timeline for d1laxa_:

• d1laxa_ first appeared in SCOP 1.65
  
• d1laxa_ appears in SCOPe 2.01
  
• d1laxa_ appears in SCOPe 2.03
  
• d1laxa_ appears in the current release, SCOPe 2.08