eF-site ID 1njt-ABCD PDB Code 1njt Chain A, B, C, D click to enlarge Title COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR Classification HYDROLASE/HYDROLASE INHIBITOR Compound Capsid protein P40 Source Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) (1NJT) Sequence A:  MDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHW LHAQVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTS PRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAG LSLSSRRCDTPFKHVALCSVGRRRGTLAVYGRDPEWVTQR FPDLTAADRDGLRAQWQRCGGDPFRSDSYGLLGNSVDALY IRERLPKLRYDKQLVGVTERESYVKA B:  TMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEH WLHAQALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTS PRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAG LSLSSRRCDTTPFKHVALCSVGRRRGTLAVYGRDPEWVTQ RFPDLTAADRDGLRAQWQRCSGDPFRSDSYGLLGNSVDAL YIRERLPKLRYDKQLVGVTERESYVKA C:  DEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWL HAALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRF LEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSL SSRRCDTTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFP DLTAADRDGLRAQWQSGDPFRSDSYGLLGNSVDALYIRER LPKLRYDKQLVGVTERESYVKA D:  DEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWL HAVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPR FLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLS LSSRRCTTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFP DLTAADRDGLRAQWQASGDPFRSDSYGLLGNSVDALYIRE RLPKLRYDKQLVGVTERESYVKA Description Functional site 1) chain A residue 62 type sequence N description BINDING SITE FOR RESIDUE CL A 257 source : AC1 2) chain A residue 161 type sequence C description BINDING SITE FOR RESIDUE CL A 257 source : AC1 3) chain A residue 162 type sequence S description BINDING SITE FOR RESIDUE CL A 257 source : AC1 4) chain A residue 224 type sequence N description BINDING SITE FOR RESIDUE CL A 257 source : AC1 5) chain B residue 362 type sequence N description BINDING SITE FOR RESIDUE CL B 2 source : AC2 6) chain B residue 461 type sequence C description BINDING SITE FOR RESIDUE CL B 2 source : AC2 7) chain B residue 462 type sequence S description BINDING SITE FOR RESIDUE CL B 2 source : AC2 8) chain B residue 524 type sequence N description BINDING SITE FOR RESIDUE CL B 2 source : AC2 9) chain C residue 1062 type sequence N description BINDING SITE FOR RESIDUE CL C 1 source : AC3 10) chain C residue 1161 type sequence C description BINDING SITE FOR RESIDUE CL C 1 source : AC3 11) chain C residue 1162 type sequence S description BINDING SITE FOR RESIDUE CL C 1 source : AC3 12) chain C residue 1224 type sequence N description BINDING SITE FOR RESIDUE CL C 1 source : AC3 13) chain D residue 1362 type sequence N description BINDING SITE FOR RESIDUE CL D 4 source : AC4 14) chain D residue 1461 type sequence C description BINDING SITE FOR RESIDUE CL D 4 source : AC4 15) chain D residue 1462 type sequence S description BINDING SITE FOR RESIDUE CL D 4 source : AC4 16) chain D residue 1524 type sequence N description BINDING SITE FOR RESIDUE CL D 4 source : AC4 17) chain A residue 31 type sequence E description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 18) chain A residue 63 type sequence H description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 19) chain A residue 132 type sequence S description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 20) chain A residue 133 type sequence L description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 21) chain A residue 134 type sequence S description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 22) chain A residue 135 type sequence S description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 23) chain A residue 136 type sequence R description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 24) chain A residue 137 type sequence R description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 25) chain A residue 164 type sequence G description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 26) chain A residue 165 type sequence R description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 27) chain A residue 166 type sequence R description BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR source : AC5 28) chain B residue 331 type sequence E description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 29) chain B residue 363 type sequence H description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 30) chain B residue 432 type sequence S description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 31) chain B residue 433 type sequence L description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 32) chain B residue 434 type sequence S description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 33) chain B residue 435 type sequence S description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 34) chain B residue 436 type sequence R description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 35) chain B residue 437 type sequence R description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 36) chain B residue 464 type sequence G description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 37) chain B residue 465 type sequence R description BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR source : AC6 38) chain C residue 1031 type sequence E description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 39) chain C residue 1063 type sequence H description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 40) chain C residue 1132 type sequence S description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 41) chain C residue 1133 type sequence L description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 42) chain C residue 1134 type sequence S description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 43) chain C residue 1135 type sequence S description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 44) chain C residue 1136 type sequence R description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 45) chain C residue 1137 type sequence R description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 46) chain C residue 1164 type sequence G description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 47) chain C residue 1165 type sequence R description BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR source : AC7 48) chain D residue 1331 type sequence E description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 49) chain D residue 1363 type sequence H description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 50) chain D residue 1432 type sequence S description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 51) chain D residue 1433 type sequence L description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 52) chain D residue 1434 type sequence S description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 53) chain D residue 1435 type sequence S description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 54) chain D residue 1436 type sequence R description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 55) chain D residue 1437 type sequence R description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 56) chain D residue 1464 type sequence G description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 57) chain D residue 1465 type sequence R description BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR source : AC8 58) chain A residue 63 type catalytic sequence H description 238 source MCSA : MCSA1 59) chain A residue 132 type catalytic sequence S description 238 source MCSA : MCSA1 60) chain A residue 134 type catalytic sequence S description 238 source MCSA : MCSA1 61) chain A residue 157 type catalytic sequence H description 238 source MCSA : MCSA1 62) chain A residue 165 type catalytic sequence R description 238 source MCSA : MCSA1 63) chain A residue 166 type catalytic sequence R description 238 source MCSA : MCSA1 64) chain B residue 363 type catalytic sequence H description 238 source MCSA : MCSA2 65) chain B residue 432 type catalytic sequence S description 238 source MCSA : MCSA2 66) chain B residue 434 type catalytic sequence S description 238 source MCSA : MCSA2 67) chain B residue 457 type catalytic sequence H description 238 source MCSA : MCSA2 68) chain B residue 465 type catalytic sequence R description 238 source MCSA : MCSA2 69) chain B residue 466 type catalytic sequence R description 238 source MCSA : MCSA2 70) chain C residue 1063 type catalytic sequence H description 238 source MCSA : MCSA3 71) chain C residue 1132 type catalytic sequence S description 238 source MCSA : MCSA3 72) chain C residue 1134 type catalytic sequence S description 238 source MCSA : MCSA3 73) chain C residue 1157 type catalytic sequence H description 238 source MCSA : MCSA3 74) chain C residue 1165 type catalytic sequence R description 238 source MCSA : MCSA3 75) chain C residue 1166 type catalytic sequence R description 238 source MCSA : MCSA3 76) chain D residue 1363 type catalytic sequence H description 238 source MCSA : MCSA4 77) chain D residue 1432 type catalytic sequence S description 238 source MCSA : MCSA4 78) chain D residue 1434 type catalytic sequence S description 238 source MCSA : MCSA4 79) chain D residue 1457 type catalytic sequence H description 238 source MCSA : MCSA4 80) chain D residue 1465 type catalytic sequence R description 238 source MCSA : MCSA4 81) chain D residue 1466 type catalytic sequence R description 238 source MCSA : MCSA4 82) chain A residue 63 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 83) chain D residue 1363 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 84) chain D residue 1432 type ACT_SITE sequence S description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 85) chain D residue 1457 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 86) chain A residue 132 type ACT_SITE sequence S description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 87) chain A residue 157 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 88) chain B residue 363 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 89) chain B residue 432 type ACT_SITE sequence S description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 90) chain B residue 457 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 91) chain C residue 1063 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 92) chain C residue 1132 type ACT_SITE sequence S description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 93) chain C residue 1157 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI1 94) chain A residue 256 type SITE sequence A description Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI2 95) chain B residue 556 type SITE sequence A description Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI2 96) chain C residue 1256 type SITE sequence A description Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI2 97) chain D residue 1556 type SITE sequence A description Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI2

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