Lineage for d2hkla1 (2hkl A:217-338)

  1. Root: SCOPe 2.07
  2. 2530962Class d: Alpha and beta proteins (a+b) [53931] (388 folds)
  3. 2616985Fold 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. 2616986Superfamily d.335.1: L,D-transpeptidase pre-catalytic domain-like [143985] (1 family) (S)
    automatically mapped to Pfam PF12229
  5. 2616987Family d.335.1.1: L,D-transpeptidase pre-catalytic domain-like [143986] (2 proteins)
  6. 2616988Protein L,D-transpeptidase, pre-catalytic domain [143987] (1 species)
  7. 2616989Species Enterococcus faecium [TaxId:1352] [143988] (2 PDB entries)
    Uniprot Q3Y185 217-338
  8. 2616991Domain d2hkla1: 2hkl A:217-338 [230766]
    Other proteins in same PDB: d2hkla2, d2hklb2, d2hklc2
    automated match to d1zata2
    complexed with so4; mutant

Details for d2hkla1

PDB Entry: 2hkl (more details), 2.6 Å

PDB Description: Crystal structure of Enterococcus faecium L,D-transpeptidase C442S mutant
PDB Compounds: (A:) L,D-transpeptidase

SCOPe Domain Sequences for d2hkla1:

Sequence; same for both SEQRES and ATOM records: (download)

>d2hkla1 d.335.1.1 (A:217-338) L,D-transpeptidase, pre-catalytic domain {Enterococcus faecium [TaxId: 1352]}

SCOPe Domain Coordinates for d2hkla1:

Click to download the PDB-style file with coordinates for d2hkla1.
(The format of our PDB-style files is described here.)

Timeline for d2hkla1: