SCOPe 2.08: Domain d2ebhx3: 2ebh X:1094-1285

Lineage for d2ebhx3 (2ebh X:1094-1285)

1. Root: SCOPe 2.08

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

3. Fold d.3: Cysteine proteinases [54000] (1 superfamily)
   consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn

4. Superfamily d.3.1: Cysteine proteinases [54001] (24 families)
   the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta-sheet

5. Family d.3.1.17: PMT C-terminal domain like [159843] (1 protein)
   displays a minimal thiol-protease fold and its catalytic triad; potential redox regulation: the catalytic cysteine can form a disulfide bond with an N-terminal cysteine

6. Protein Dermonecrotic toxin, ToxA [159844] (1 species)
   Synonym: Mitogenic toxin PMT

7. Species Pasteurella multocida [TaxId:747] [159845] (3 PDB entries)
   Uniprot P17452 1094-1285

8. Domain d2ebhx3: 2ebh X:1094-1285 [146771]
   Other proteins in same PDB: d2ebhx1, d2ebhx2

Details for d2ebhx3

PDB Entry: 2ebh, 2.4 Å

PDB Description: crystal structures reveal a thiol-protease like catalytic triad in the c-terminal region of pasteurella multocida toxin

PDB Compounds: (X:) Dermonecrotic toxin

SCOPe Domain Sequences for d2ebhx3:

Sequence; same for both SEQRES and ATOM records:

>d2ebhx3 d.3.1.17 (X:1094-1285) Dermonecrotic toxin, ToxA {Pasteurella multocida [TaxId: 747]}
lenwqvltppqgkilglkqfkltagfpteqsrlpllensvsedlreelmqkidaikndvk
mnslvcmeagssdsvspkvaarlkdmgleagmgasitwwrreggmefshqmhttasfkfa
gkefavdashlqfvhdqldttililpvddwaleiaqrnrainpfveyvsktgnmlalfmp
plftkprltral

Timeline for d2ebhx3:

• d2ebhx3 first appeared in SCOP 1.75
  
• d2ebhx3 appears in SCOPe 2.07