1BFZ
BOUND CONFORMATION OF N-TERMINAL CLEAVAGE PRODUCT PEPTIDE MIMIC (P1-P9 OF RELEASE SITE) WHILE BOUND TO HCMV PROTEASE AS DETERMINED BY TRANSFERRED NOESY EXPERIMENTS (P1-P5 SHOWN ONLY), NMR, 32 STRUCTURES
Summary for 1BFZ
Entry DOI | 10.2210/pdb1bfz/pdb |
Descriptor | HCMV PROTEASE R-SITE N-TERMINAL CLEAVAGE PRODUCT (1 entity in total) |
Functional Keywords | substriate cleavage, bound conformation, extended conformation, substrate-based competitive inhibitor design, peptide |
Total number of polymer chains | 1 |
Total formula weight | 593.69 |
Authors | Laplante, S.R.,Aubry, N.,Bonneau, P.R.,Cameron, D.R.,Lagace, L.,Massariol, M.-J.,Montpetit, H.,Ploufe, C.,Kawai, S.H.,Fulton, B.D.,Chen, Z.,Ni, F. (deposition date: 1998-05-25, release date: 1999-05-25, Last modification date: 2024-06-05) |
Primary citation | LaPlante, S.R.,Aubry, N.,Bonneau, P.R.,Cameron, D.R.,Lagace, L.,Massariol, M.J.,Montpetit, H.,Plouffe, C.,Kawai, S.H.,Fulton, B.D.,Chen, Z.,Ni, F. Human cytomegalovirus protease complexes its substrate recognition sequences in an extended peptide conformation. Biochemistry, 37:9793-9801, 1998 Cited by PubMed: 9657693DOI: 10.1021/bi980555v PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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