Lineage for d2hkla2 (2hkl A:339-466)

  1. Root: SCOPe 2.06
  2. 2017114Class b: All beta proteins [48724] (177 folds)
  3. 2078210Fold b.160: L,D-transpeptidase catalytic domain-like [141522] (1 superfamily)
    barrel, closed; n=8, S=10; one overside connection
  4. 2078211Superfamily b.160.1: L,D-transpeptidase catalytic domain-like [141523] (1 family) (S)
    automatically mapped to Pfam PF03734
  5. 2078212Family b.160.1.1: L,D-transpeptidase catalytic domain-like [141524] (3 protein domains)
    Pfam PF03734; ErfK/YbiS/YcfS/YnhG
  6. 2078217Protein L,D-transpeptidase, C-terminal, catalytic domain [141525] (1 species)
  7. 2078218Species Enterococcus faecium [TaxId:1352] [141526] (2 PDB entries)
    Uniprot Q3Y185 339-466
  8. 2078220Domain d2hkla2: 2hkl A:339-466 [230767]
    Other proteins in same PDB: d2hkla1, d2hklb1, d2hklc1
    automated match to d1zata1
    complexed with so4; mutant

Details for d2hkla2

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 d2hkla2:

Sequence, based on SEQRES records: (download)

>d2hkla2 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)

>d2hkla2 b.160.1.1 (A:339-466) L,D-transpeptidase, C-terminal, catalytic domain {Enterococcus faecium [TaxId: 1352]}

SCOPe Domain Coordinates for d2hkla2:

Click to download the PDB-style file with coordinates for d2hkla2.
(The format of our PDB-style files is described here.)

Timeline for d2hkla2: