eF-site ID 1rgq-A PDB Code 1rgq Chain A click to enlarge Title M9A HCV Protease complex with pentapeptide keto-amide inhibitor Classification Viral protein, hydrolase Compound NS3 Protease Source Hepatitis C virus genotype 1a (isolate H) (HCV) (O39914_9HEPC) Sequence A:  QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASP KGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLV TRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA GHAVGLFRAAVCTRGVTKAVDFIPVENLETTMRS Description (1)  NS3 Protease (E.C.3.4.21.98), NS4A peptide Functional site 1) chain A residue 100 type sequence C description BINDING SITE FOR RESIDUE ZN A 193 source : AC1 2) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE ZN A 193 source : AC1 3) chain A residue 102 type sequence C description BINDING SITE FOR RESIDUE ZN A 193 source : AC1 4) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 193 source : AC1 5) chain A residue 61 type catalytic sequence G description 776 source MCSA : MCSA1 6) chain A residue 85 type catalytic sequence L description 776 source MCSA : MCSA1 7) chain A residue 141 type catalytic sequence S description 776 source MCSA : MCSA1 8) chain A residue 143 type catalytic sequence G description 776 source MCSA : MCSA1 9) chain A residue 61 type ACT_SITE sequence G description Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 85 type ACT_SITE sequence L description Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 143 type ACT_SITE sequence G description Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8248148, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 101 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI source Swiss-Prot : SWS_FT_FI4 13) chain A residue 103 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI source Swiss-Prot : SWS_FT_FI4 14) chain A residue 149 type BINDING sequence P description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI source Swiss-Prot : SWS_FT_FI5 15) chain A residue 153 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 source Swiss-Prot : SWS_FT_FI6

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