eF-site ID 2oc8-ABCD PDB Code 2oc8 Chain A, B, C, D click to enlarge Title Structure of Hepatitis C Viral NS3 protease domain complexed with NS4A peptide and ketoamide SCH503034 Classification VIRAL PROTEIN Compound Hepatitis C virus Source (Q9QP06_9HEPC) Sequence A:  MGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVST ATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNV DQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRR RGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAV CTRGVAKAVDFIPVENLETTMRS B:  KGSVVIVGRIVLSGKPAIIPKK C:  QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASP KGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLV TRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA GHAVGLFRAAVCTRGVAKAVDFIPVENLETTM D:  KGSVVIVGRIVLSGKPA 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 13 type sequence L description BINDING SITE FOR RESIDUE BME A 801 source : AC3 8) chain A residue 16 type sequence C description BINDING SITE FOR RESIDUE BME A 801 source : AC3 9) chain A residue 17 type sequence I description BINDING SITE FOR RESIDUE BME A 801 source : AC3 10) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE BME A 801 source : AC3 11) chain A residue 41 type sequence Q description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 12) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 13) chain A residue 123 type sequence R description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 14) chain A residue 132 type sequence I description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 15) chain A residue 135 type sequence L description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 16) chain A residue 137 type sequence G description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 17) chain A residue 138 type sequence S description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 18) chain A residue 139 type sequence S description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 19) chain A residue 154 type sequence F description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 20) chain A residue 155 type sequence R description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 21) chain A residue 156 type sequence A description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 22) chain A residue 157 type sequence A description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 23) chain A residue 158 type sequence V description BINDING SITE FOR RESIDUE U5G A 999 source : AC4 24) chain A residue 57 type catalytic sequence H description 776 source MCSA : MCSA1 25) chain A residue 81 type catalytic sequence D description 776 source MCSA : MCSA1 26) chain A residue 137 type catalytic sequence G description 776 source MCSA : MCSA1 27) chain A residue 139 type catalytic sequence S description 776 source MCSA : MCSA1 28) chain C residue 57 type catalytic sequence H description 776 source MCSA : MCSA2 29) chain C residue 81 type catalytic sequence D description 776 source MCSA : MCSA2 30) chain C residue 137 type catalytic sequence G description 776 source MCSA : MCSA2 31) chain C residue 139 type catalytic sequence S description 776 source MCSA : MCSA2 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) 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 44) 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 45) 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

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