eF-site ID 1jq7-AB PDB Code 1jq7 Chain A, B click to enlarge Title HCMV protease dimer-interface mutant, S225Y complexed to Inhibitor BILC 408 Classification HYDROLASE/HYDROLASE INHIBITOR Compound ASSEMBLIN Source Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5) (VP40_HCMVA) Sequence A:  QSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLSVA LPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEI VRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSP FKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDG LRAQWDPFRSDSYGLLGNYVDALYIRERLPKLRYDKQLVG VTERESYVKA B:  QSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLALP LNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVR RASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRC DTTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAA DRDGLRAQWQSGDPFRSDSYGLLGNYVDALYIRERLPKLR YDKQLVGVTERESYVKA Description Functional site 1) chain A residue 1031 type sequence E description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 2) chain A residue 1062 type sequence N description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 3) chain A residue 1063 type sequence H description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 4) chain A residue 1132 type sequence S description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 5) chain A residue 1133 type sequence L description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 6) chain A residue 1134 type sequence S description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 7) chain A residue 1135 type sequence S description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 8) chain A residue 1161 type sequence C description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 9) chain A residue 1163 type sequence V description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 10) chain A residue 1164 type sequence G description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 11) chain A residue 1165 type sequence R description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 12) chain A residue 1166 type sequence R description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 13) chain A residue 1231 type sequence I description BINDING SITE FOR RESIDUE 0FP A 261 source : AC1 14) chain B residue 1331 type sequence E description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 15) chain B residue 1362 type sequence N description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 16) chain B residue 1363 type sequence H description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 17) chain B residue 1432 type sequence S description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 18) chain B residue 1433 type sequence L description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 19) chain B residue 1434 type sequence S description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 20) chain B residue 1435 type sequence S description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 21) chain B residue 1436 type sequence R description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 22) chain B residue 1456 type sequence K description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 23) chain B residue 1463 type sequence V description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 24) chain B residue 1464 type sequence G description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 25) chain B residue 1465 type sequence R description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 26) chain B residue 1531 type sequence I description BINDING SITE FOR RESIDUE 0FP B 561 source : AC2 27) chain A residue 1063 type catalytic sequence H description 238 source MCSA : MCSA1 28) chain A residue 1132 type catalytic sequence S description 238 source MCSA : MCSA1 29) chain A residue 1134 type catalytic sequence S description 238 source MCSA : MCSA1 30) chain A residue 1157 type catalytic sequence H description 238 source MCSA : MCSA1 31) chain A residue 1165 type catalytic sequence R description 238 source MCSA : MCSA1 32) chain A residue 1166 type catalytic sequence R description 238 source MCSA : MCSA1 33) chain B residue 1363 type catalytic sequence H description 238 source MCSA : MCSA2 34) chain B residue 1432 type catalytic sequence S description 238 source MCSA : MCSA2 35) chain B residue 1434 type catalytic sequence S description 238 source MCSA : MCSA2 36) chain B residue 1457 type catalytic sequence H description 238 source MCSA : MCSA2 37) chain B residue 1465 type catalytic sequence R description 238 source MCSA : MCSA2 38) chain B residue 1466 type catalytic sequence R description 238 source MCSA : MCSA2 39) chain A residue 1063 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:8805706 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 1132 type ACT_SITE sequence S description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:8805706 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 1363 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:8805706 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 1432 type ACT_SITE sequence S description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:8805706 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 1157 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 1457 type ACT_SITE sequence H description Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 1256 type SITE sequence A description Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI5 46) chain B residue 1556 type SITE sequence A description Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 source Swiss-Prot : SWS_FT_FI5

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