eF-site ID 2f9v-ABCD PDB Code 2f9v Chain A, B, C, D click to enlarge Title HCV NS3 protease domain with NS4a peptide and a ketoamide inhibitor with P1 and P2 cyclopropylalannines Classification VIRAL PROTEIN Compound NS3 protease/helicase Source (AAT94284) Sequence A:  MGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVST ATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNV DQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRR RGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAV CTRGVAKAVDFIPVENLETTMRS B:  KGSVVIVGRIVLSGKPAIIPKK C:  QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASP KGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLV TRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA GHAVGLFRAAVCTRGVAKAVDFIPVENLETTM 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 41 type sequence Q description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 8) chain A residue 42 type sequence T description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 9) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 10) chain A residue 132 type sequence I description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 11) chain A residue 136 type sequence K description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 12) chain A residue 137 type sequence G description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 13) chain A residue 138 type sequence S description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 14) chain A residue 139 type sequence S description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 15) chain A residue 155 type sequence R description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 16) chain A residue 156 type sequence A description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 17) chain A residue 157 type sequence A description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 18) chain A residue 159 type sequence C description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 19) chain A residue 168 type sequence D description BINDING SITE FOR RESIDUE BN6 A 999 source : AC3 20) chain A residue 57 type catalytic sequence H description 776 source MCSA : MCSA1 21) chain A residue 81 type catalytic sequence D description 776 source MCSA : MCSA1 22) chain A residue 137 type catalytic sequence G description 776 source MCSA : MCSA1 23) chain A residue 139 type catalytic sequence S description 776 source MCSA : MCSA1 24) chain C residue 57 type catalytic sequence H description 776 source MCSA : MCSA2 25) chain C residue 81 type catalytic sequence D description 776 source MCSA : MCSA2 26) chain C residue 137 type catalytic sequence G description 776 source MCSA : MCSA2 27) chain C residue 139 type catalytic sequence S description 776 source MCSA : MCSA2 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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

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