SCOPe 2.02: Domain d4uaga3: 4uag A:94-297

Lineage for d4uaga3 (4uag A:94-297)

1. Root: SCOPe 2.02

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-acetylmuramoyl-L-alanine:D-glutamate ligase MurD [53625] (1 species)

7. Species Escherichia coli [TaxId:562] [53626] (11 PDB entries)

8. Domain d4uaga3: 4uag A:94-297 [34955]
   Other proteins in same PDB: d4uaga1, d4uaga2
   complexed with so4, uag, unx

Details for d4uaga3

PDB Entry: 4uag, 1.66 Å

PDB Description: udp-n-acetylmuramoyl-l-alanine:d-glutamate ligase

PDB Compounds: (A:) udp-n-acetylmuramoyl-l-alanine:d-glutamate ligase

SCOPe Domain Sequences for d4uaga3:

Sequence, based on SEQRES records:

>d4uaga3 c.72.2.1 (A:94-297) UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase MurD {Escherichia coli [TaxId: 562]}
dielfcreaqapivaitgsngkstvttlvgemakaagvnvgvggniglpalmllddecel
yvlelssfqlettsslqavaatilnvtedhmdrypfglqqyraaklriyenakvcvvnad
daltmpirgadercvsfgvnmgdyhlnhqqgetwlrvkgekvlnvkemklsgqhnytnal
aalaladaaglprasslkalttft

Sequence, based on observed residues (ATOM records):

>d4uaga3 c.72.2.1 (A:94-297) UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase MurD {Escherichia coli [TaxId: 562]}
dielfcreaqapivaitgsngkstvttlvgemakaagvnvgvggniglpalmllddecel
yvlelssfqlettsslqavaatilnvtedhmdrypfglqqyraaklriyenakvcvvnad
daltmpircvsfgvnmgdyhlnhetwlrvkgekvlnvkemklsgqhnytnalaalalada
aglprasslkalttft

Timeline for d4uaga3:

• d4uaga3 first appeared (with stable ids) in SCOP 1.55
  
• d4uaga3 appears in SCOPe 2.01
  
• d4uaga3 appears in SCOPe 2.03
  
• d4uaga3 appears in the current release, SCOPe 2.08