eF-site ID 2oc0-ABCD PDB Code 2oc0 Chain A, B, C, D click to enlarge Title Structure of NS3 complexed with a ketoamide inhibitor SCh491762 Classification VIRAL PROTEIN Compound Hepatitis C Virus Source Hepatitis C virus subtype 1a (Q9QP06_9HEPC) Sequence A:  APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAT QTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQ DLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRG DSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCT RGVAKAVDFIPVENLETTMRS B:  KGSVVIVGRIVLSGKPAIIPKK C:  VEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPK GPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVT RHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAG HAVGLFRAAVCTRGVAKAVDFIPVENLETTM D:  GSVVIVGRIVLSGKPA Description Functional site 1) chain A residue 97 type sequence C description BINDING SITE FOR RESIDUE ZN A 901 source : AC1 2) chain A residue 99 type sequence C description BINDING SITE FOR RESIDUE ZN A 901 source : AC1 3) chain A residue 145 type sequence C description BINDING SITE FOR RESIDUE ZN A 901 source : AC1 4) chain C residue 97 type sequence C description BINDING SITE FOR RESIDUE ZN C 902 source : AC2 5) chain C residue 99 type sequence C description BINDING SITE FOR RESIDUE ZN C 902 source : AC2 6) chain C residue 145 type sequence C description BINDING SITE FOR RESIDUE ZN C 902 source : AC2 7) chain A residue 16 type sequence C description BINDING SITE FOR RESIDUE BME A 801 source : AC3 8) chain A residue 17 type sequence I description BINDING SITE FOR RESIDUE BME A 801 source : AC3 9) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE BME A 801 source : AC3 10) chain A residue 41 type sequence Q description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 11) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 12) chain A residue 132 type sequence I description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 13) chain A residue 136 type sequence K description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 14) chain A residue 137 type sequence G description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 15) chain A residue 138 type sequence S description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 16) chain A residue 139 type sequence S description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 17) chain A residue 154 type sequence F description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 18) chain A residue 155 type sequence R description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 19) chain A residue 156 type sequence A description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 20) chain A residue 157 type sequence A description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 21) chain A residue 159 type sequence C description BINDING SITE FOR RESIDUE HU1 A 999 source : AC4 22) chain A residue 57 type ACT_SITE sequence H 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 23) chain C residue 57 type ACT_SITE sequence H 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 24) chain A residue 81 type ACT_SITE sequence D description Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 81 type ACT_SITE sequence D description Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 139 type ACT_SITE sequence S 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 27) chain C residue 139 type ACT_SITE sequence S 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 28) chain A residue 149 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 source Swiss-Prot : SWS_FT_FI6 29) chain C residue 149 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 97 type BINDING sequence C 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 31) chain A residue 99 type BINDING sequence C 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 32) chain C residue 97 type BINDING sequence C 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 33) chain C residue 99 type BINDING sequence C 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 34) chain A residue 145 type BINDING sequence C 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 35) chain C residue 145 type BINDING sequence C 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 36) chain A residue 57 type catalytic sequence H description 776 source MCSA : MCSA1 37) chain A residue 81 type catalytic sequence D description 776 source MCSA : MCSA1 38) chain A residue 137 type catalytic sequence G description 776 source MCSA : MCSA1 39) chain A residue 139 type catalytic sequence S description 776 source MCSA : MCSA1 40) chain C residue 57 type catalytic sequence H description 776 source MCSA : MCSA2 41) chain C residue 81 type catalytic sequence D description 776 source MCSA : MCSA2 42) chain C residue 137 type catalytic sequence G description 776 source MCSA : MCSA2 43) chain C residue 139 type catalytic sequence S description 776 source MCSA : MCSA2

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