SCOPe 2.08: Domain d2hklc1: 2hkl C:217-338

Lineage for d2hklc1 (2hkl C:217-338)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.335: L,D-transpeptidase pre-catalytic domain-like [143984] (1 superfamily)
   unusual fold, made of four helices and four 2-3 stranded beta-sheets

4. Superfamily d.335.1: L,D-transpeptidase pre-catalytic domain-like [143985] (1 family)
   automatically mapped to Pfam PF12229

5. Family d.335.1.1: L,D-transpeptidase pre-catalytic domain-like [143986] (2 proteins)

6. Protein L,D-transpeptidase, pre-catalytic domain [143987] (1 species)

7. Species Enterococcus faecium [TaxId:1352] [143988] (2 PDB entries)
   Uniprot Q3Y185 217-338

8. Domain d2hklc1: 2hkl C:217-338 [230770]
   Other proteins in same PDB: d2hkla2, d2hklb2, d2hklc2
   automated match to d1zata2
   complexed with so4; mutant

Details for d2hklc1

PDB Entry: 2hkl, 2.6 Å

PDB Description: crystal structure of enterococcus faecium l,d-transpeptidase c442s mutant

PDB Compounds: (C:) L,D-transpeptidase

SCOPe Domain Sequences for d2hklc1:

Sequence; same for both SEQRES and ATOM records:

>d2hklc1 d.335.1.1 (C:217-338) L,D-transpeptidase, pre-catalytic domain {Enterococcus faecium [TaxId: 1352]}
keqlasmnaianvkatysingetfqipssdimswltyndgkvdldteqvrqyvtdlgtky
ntstndtkfkstkrgevtvpvgtyswtiqtdsetealkkailagqdftrspivqggttad
hp

Timeline for d2hklc1:

• d2hklc1 first appeared in SCOPe 2.03
  
• d2hklc1 appears in SCOPe 2.07