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1CQQ

TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR

Summary for 1CQQ
Entry DOI10.2210/pdb1cqq/pdb
DescriptorTYPE 2 RHINOVIRUS 3C PROTEASE, 4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC ACID ETHYL ESTER (3 entities in total)
Functional Keywordsviral protein, hydrolase
Biological sourceHuman rhinovirus 2
Cellular locationCapsid protein VP0: Virion . Capsid protein VP4: Virion . Capsid protein VP2: Virion . Capsid protein VP3: Virion . Capsid protein VP1: Virion . Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion . Protease 3C: Host cytoplasm . Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P04936
Total number of polymer chains1
Total formula weight20582.34
Authors
Matthews, D.,Ferre, R.A. (deposition date: 1999-08-10, release date: 1999-09-20, Last modification date: 2018-01-31)
Primary citationMatthews, D.A.,Dragovich, P.S.,Webber, S.E.,Fuhrman, S.A.,Patick, A.K.,Zalman, L.S.,Hendrickson, T.F.,Love, R.A.,Prins, T.J.,Marakovits, J.T.,Zhou, R.,Tikhe, J.,Ford, C.E.,Meador, J.W.,Ferre, R.A.,Brown, E.L.,Binford, S.L.,Brothers, M.A.,DeLisle, D.M.,Worland, S.T.
Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes.
Proc.Natl.Acad.Sci.USA, 96:11000-11007, 1999
Cited by
PubMed: 10500114
DOI: 10.1073/pnas.96.20.11000
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

217705

數據於2024-03-27公開中

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