SCOP 1.75: Domain d1e8cb3: 1e8c B:104-337

Lineage for d1e8cb3 (1e8c B:104-337)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.72: Ribokinase-like [53612] (3 superfamilies)
   core: 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest
   potential superfamily: members of this fold have similar functions but different ATP-binding sites

4. Superfamily c.72.2: MurD-like peptide ligases, catalytic domain [53623] (2 families)
   has extra strand located between strands 1 and 2

5. Family c.72.2.1: MurCDEF [53624] (4 proteins)

6. Protein UDP-N-acetylmuramyl tripeptide synthetase MurE [64150] (1 species)

7. Species Escherichia coli [TaxId:562] [64151] (1 PDB entry)

8. Domain d1e8cb3: 1e8c B:104-337 [59382]
   Other proteins in same PDB: d1e8ca1, d1e8ca2, d1e8cb1, d1e8cb2
   complexed with api, cl, uag

Details for d1e8cb3

PDB Entry: 1e8c, 2 Å

PDB Description: structure of mure the udp-n-acetylmuramyl tripeptide synthetase from e. coli

PDB Compounds: (B:) udp-n-acetylmuramoylalanyl-d-glutamate--2,6-diaminopimelate ligase

SCOP Domain Sequences for d1e8cb3:

Sequence; same for both SEQRES and ATOM records:

>d1e8cb3 c.72.2.1 (B:104-337) UDP-N-acetylmuramyl tripeptide synthetase MurE {Escherichia coli [TaxId: 562]}
psdnlrlvgvtgtngkttttqllaqwsqllgeisavmgtvgngllgkviptenttgsavd
vqhelaglvdqgatfcamevsshglvqhrvaalkfaasvftnlsrdhldyhgdmehyeaa
kwllysehhcgqaiinaddevgrrwlaklpdavavsmedhinpnchgrwlkatevnyhds
gatirfssswgdgeieshlmgafnvsnlllalatllalgypladllktaarlqp

Timeline for d1e8cb3:

• d1e8cb3 first appeared in SCOP 1.57
  
• d1e8cb3 appears in SCOP 1.73
  
• d1e8cb3 appears in SCOPe 2.01
  
• d1e8cb3 appears in the current release, SCOPe 2.08