eF-site ID 2xni-ABCD PDB Code 2xni Chain A, B, C, D click to enlarge Title Protein-ligand complex of a novel macrocyclic HCV NS3 protease inhibitor derived from amino cyclic boronates Classification HYDROLASE/HYDROLASE REGULATOR Compound NS3 PROTEASE Source Hepatitis C virus (C9WU77_9HEPC) Sequence A:  GAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTA TQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVD QDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRR GDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAAVC TRGVAKAVDFIPVENLETTMR B:  QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASP KGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLV TRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA GHAVGLFRAAVCTRGVAKAVDFIPVENLETTMR C:  KGSVVIVGRIVLSGKPAIIPK D:  GSVVIVGRIVLSGKPA Description (1)  NS3 PROTEASE, NS4A COFACTOR Functional site 1) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 2) chain A residue 123 type sequence R description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 3) chain A residue 135 type sequence L description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 4) chain A residue 137 type sequence G description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 5) chain A residue 139 type sequence S description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 6) chain A residue 154 type sequence F description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 7) chain A residue 155 type sequence R description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 8) chain A residue 156 type sequence A description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 9) chain A residue 157 type sequence A description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 10) chain A residue 168 type sequence D description BINDING SITE FOR RESIDUE TR8 A 1181 source : AC1 11) chain A residue 97 type sequence C description BINDING SITE FOR RESIDUE ZN A 1182 source : AC2 12) chain A residue 98 type sequence T description BINDING SITE FOR RESIDUE ZN A 1182 source : AC2 13) chain A residue 99 type sequence C description BINDING SITE FOR RESIDUE ZN A 1182 source : AC2 14) chain A residue 145 type sequence C description BINDING SITE FOR RESIDUE ZN A 1182 source : AC2 15) chain B residue 97 type sequence C description BINDING SITE FOR RESIDUE ZN B 1181 source : AC3 16) chain B residue 98 type sequence T description BINDING SITE FOR RESIDUE ZN B 1181 source : AC3 17) chain B residue 99 type sequence C description BINDING SITE FOR RESIDUE ZN B 1181 source : AC3 18) chain B residue 145 type sequence C description BINDING SITE FOR RESIDUE ZN B 1181 source : AC3 19) chain A residue 5 type sequence A description BINDING SITE FOR RESIDUE MG A 1183 source : AC4 20) chain A residue 111 type sequence A description BINDING SITE FOR RESIDUE MG A 1183 source : AC4 21) chain A residue 4 type sequence T description BINDING SITE FOR RESIDUE MG C 1041 source : AC5 22) chain C residue 31 type sequence L description BINDING SITE FOR RESIDUE MG C 1041 source : AC5 23) chain C residue 33 type sequence G description BINDING SITE FOR RESIDUE MG C 1041 source : AC5 24) chain D residue 32 type sequence S description BINDING SITE FOR RESIDUE MG C 1041 source : AC5 25) chain A residue 57 type catalytic sequence H description 776 source MCSA : MCSA1 26) chain A residue 81 type catalytic sequence D description 776 source MCSA : MCSA1 27) chain A residue 137 type catalytic sequence G description 776 source MCSA : MCSA1 28) chain A residue 139 type catalytic sequence S description 776 source MCSA : MCSA1 29) chain B residue 57 type catalytic sequence H description 776 source MCSA : MCSA2 30) chain B residue 81 type catalytic sequence D description 776 source MCSA : MCSA2 31) chain B residue 137 type catalytic sequence G description 776 source MCSA : MCSA2 32) chain B residue 139 type catalytic sequence S description 776 source MCSA : MCSA2 33) 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 34) 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 35) chain B 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 36) chain B 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 37) 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 38) chain B 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 39) 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 40) chain B residue 149 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 source Swiss-Prot : SWS_FT_FI6 41) 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 42) chain B 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 43) 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 44) chain B 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 45) 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 46) chain B 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

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