Structural Classification of Proteins




Fold: Cysteine proteinases
- consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn
Lineage:
- Root: scop
- Class: Alpha and beta proteins (a+b)
Mainly antiparallel beta sheets (segregated alpha and beta regions)
- Fold: Cysteine proteinases
consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn
Superfamilies:
- 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
- Papain-like (19)


- FMDV leader protease (1)

- Calpain large subunit, catalytic domain (domain II) (2)

- Transglutaminase (1)


- Arylamine N-acetyltransferase (1)

fold similar to that of the factor XIII catalytic domain
- Deubiquitinating enzyme (2)

- Adenoviral protease-like (2)

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