Lineage for d1zata1 (1zat A:339-466)

  1. Root: SCOP 1.73
  2. 651986Class b: All beta proteins [48724] (165 folds)
  3. 681000Fold b.160: L,D-transpeptidase catalytic domain-like [141522] (1 superfamily)
    barrel, closed; n=8, S=10; one overside connection
  4. 681001Superfamily b.160.1: L,D-transpeptidase catalytic domain-like [141523] (1 family) (S)
  5. 681002Family b.160.1.1: L,D-transpeptidase catalytic domain-like [141524] (2 proteins)
    Pfam PF03734; ErfK/YbiS/YcfS/YnhG
  6. 681007Protein L,D-transpeptidase, C-terminal, catalytic domain [141525] (1 species)
  7. 681008Species Enterococcus faecium [TaxId:1352] [141526] (1 PDB entry)
  8. 681009Domain d1zata1: 1zat A:339-466 [124845]
    Other proteins in same PDB: d1zata2
    complexed with so4, zn

Details for d1zata1

PDB Entry: 1zat (more details), 2.4 Å

PDB Description: Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A resolution
PDB Compounds: (A:) L,D-transpeptidase

SCOP Domain Sequences for d1zata1:

Sequence, based on SEQRES records: (download)

>d1zata1 b.160.1.1 (A:339-466) L,D-transpeptidase, C-terminal, catalytic domain {Enterococcus faecium [TaxId: 1352]}

Sequence, based on observed residues (ATOM records): (download)

>d1zata1 b.160.1.1 (A:339-466) L,D-transpeptidase, C-terminal, catalytic domain {Enterococcus faecium [TaxId: 1352]}

SCOP Domain Coordinates for d1zata1:

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Timeline for d1zata1:

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