Motion in Aspartic Proteases, besides endothiapepsin: Penicllopepsin, Rhizopuspepsin, Chymosin, Porcine Pepsin [dprotase]

[ jump to morphs ]

Classification Suspected Domain Motion, Shear Mechanism [D-s-2]

Structures 1PSG Conformation 5 2APP Conformation 1 2APR Conformation 2 [ PartsList ] 5PEP Porcine pepsin [ PartsList ] 3CMS Conformation 4 [ PartsList ] 4PEP Porcine pepsin [ PartsList ]

Description Similar to endothiapepsin. Many intermediate conformations observed.

Particular values describing motion Experimental Methods = x (Traditional x-ray) Creation Date = 19970822 Modification Date = 19970822

References A Sali, B Veerapandian, J B Cooper, D S Moss, T Hofmann and T L Blundell (1992). Domain Flexibility in Aspartic Proteases. Proteins: Struc. Func. Genet. 12: 158-170. [Medline info for 92294166]

GO terms associated with structures Molecular function aspartic-type endopeptidase activity, pepsin A activity Biological process proteolysis and peptidolysis

Morphs

[ show all images ]

Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

---

Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu