SCOPe 2.08: Domain d1zata1: 1zat A:339-466

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

1. Root: SCOPe 2.08

2. Class b: All beta proteins [48724] (180 folds)

3. Fold b.160: L,D-transpeptidase catalytic domain-like [141522] (1 superfamily)
   barrel, closed; n=8, S=10; one overside connection

4. Superfamily b.160.1: L,D-transpeptidase catalytic domain-like [141523] (1 family)
   automatically mapped to Pfam PF03734

5. Family b.160.1.1: L,D-transpeptidase catalytic domain-like [141524] (3 proteins)
   Pfam PF03734; ErfK/YbiS/YcfS/YnhG

6. Protein L,D-transpeptidase, C-terminal, catalytic domain [141525] (2 species)

7. Species Enterococcus faecium [TaxId:1352] [141526] (2 PDB entries)
   Uniprot Q3Y185 339-466

8. Domain d1zata1: 1zat A:339-466 [124845]
   Other proteins in same PDB: d1zata2
   complexed with so4, zn

Details for d1zata1

PDB Entry: 1zat, 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

SCOPe Domain Sequences for d1zata1:

Sequence, based on SEQRES records:

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

Sequence, based on observed residues (ATOM records):

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

Timeline for d1zata1:

• d1zata1 first appeared in SCOP 1.73
  
• d1zata1 appears in SCOPe 2.07