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

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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 functionaspartic-type endopeptidase activity, pepsin A activity
Biological processproteolysis and peptidolysis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
pepsinogen upload [ A ] 4pep [ A ] 326

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
88217-27688 pepsin upload [ A ] upload [ E ] 326
88569-28414 pepsin with seqres 1psn [ A ] 1pso [ E ] 326


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