Structural Classification of Proteins
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Fold: Cysteine proteinases

consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b)
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Cysteine proteinases
    consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn

Superfamilies:

  1. Cysteine proteinases (7)
    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
    1. Papain-like (19) pic
    2. FMDV leader protease (1)
    3. Calpain large subunit, catalytic domain (domain II) (2)
    4. Transglutaminase (1) pic
    5. Arylamine N-acetyltransferase (1)
      fold similar to that of the factor XIII catalytic domain
    6. Deubiquitinating enzyme (2)
    7. Adenoviral protease-like (2)

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Generated from scop database 1.55 with scopm 1.095 on Mon Jul 9 18:35:50 2001
Copyright © 1994-2001 The scop authors / scop@mrc-lmb.cam.ac.uk