1N1L

CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X)

Summary for 1N1L

• Entry DOI: 10.2210/pdb1n1l/pdb
• Descriptor: HCV NS3 SERINE PROTEASE, NS4A COFACTOR, ZINC ION, ... (5 entities in total)
• Functional Keywords: viral protein, serine protease, nonstructural proteins, cofactor peptide, helicase, inhibitor
• Biological source: Hepatitis C virus; More
• Cellular location: Core protein p21: Host endoplasmic reticulum membrane ; Single-pass membrane protein . Core protein p19: Virion . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . p7: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Protease NS2-3: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein : P27958
• Total number of polymer chains: 4
• Total formula weight: 47442.41

Authors

Andrews, D.M.,Chaignot, H.,Coomber, B.A.,Good, A.C.,Hind, S.L.,Jones, P.S.,Mill, G.,Robinson, J.E.,Skarzynski, T.,Slater, M.J.,Somers, D.O.N. (deposition date: 2002-10-18, release date: 2003-10-21, Last modification date: 2021-10-27)

Primary citation

Andrews, D.M.,Chaignot, H.,Coomber, B.A.,Good, A.C.,Hind, S.L.,Johnson, M.R.,Jones, P.S.,Mill, G.,Robinson, J.E.,Skarzynski, T.,Slater, M.J.,Somers, D.O.N.
Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray Crystal Structure Data in the Optimisation of P3 and P4 Substituents
Org.Lett., 4:4479-4482, 2002

PubMed Abstract: [reaction: see text] In this, the second of two letters, we describe the elaboration of the pyrrolidine-5,5-trans-lactam template to delineate the requirements for optimal substitution of the pyrrolidine and lactam nitrogen atoms. Central to the strategy is the use of rapid iterative synthesis in conjunction with X-ray crystal structure determination of ligand-protein complexes.

PubMed: 12465917
DOI: 10.1021/ol027014p

Experimental method

X-RAY DIFFRACTION (2.6 Å)