eF-site ID 1fkn-ABCD PDB Code 1fkn Chain A, B, C, D click to enlarge Title Structure of Beta-Secretase Complexed with Inhibitor Classification HYDROLASE/HYDROLASE INHIBITOR Compound MEMAPSIN 2 Source Homo sapiens (Human) (1FKN) Sequence A:  RRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTG SSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQG KWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSN WEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQL CGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIR REWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNL RLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGT TPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVAT SQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGF AVSACHVHDEFRTAAVEGPFVTLDMEDCGYN B:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN C:  EVNXAEF D:  EVNXAEF Description Functional site 1) chain A residue 10 type sequence S description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 2) chain A residue 11 type sequence G description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 3) chain A residue 32 type sequence D description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 4) chain A residue 34 type sequence G description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 5) chain A residue 35 type sequence S description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 6) chain A residue 70 type sequence P description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 7) chain A residue 71 type sequence Y description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 8) chain A residue 72 type sequence T description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 9) chain A residue 73 type sequence Q description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 10) chain A residue 108 type sequence F description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 11) chain A residue 110 type sequence I description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 12) chain A residue 198 type sequence Y description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 13) chain A residue 224 type sequence K description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 14) chain A residue 228 type sequence D description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 15) chain A residue 230 type sequence G description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 16) chain A residue 231 type sequence T description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 17) chain A residue 232 type sequence T description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 18) chain A residue 235 type sequence R description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 19) chain A residue 329 type sequence T description BINDING SITE FOR CHAIN C OF INHIBITOR source : AC1 20) chain B residue 10 type sequence S description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 21) chain B residue 11 type sequence G description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 22) chain B residue 32 type sequence D description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 23) chain B residue 34 type sequence G description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 24) chain B residue 35 type sequence S description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 25) chain B residue 70 type sequence P description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 26) chain B residue 71 type sequence Y description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 27) chain B residue 72 type sequence T description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 28) chain B residue 73 type sequence Q description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 29) chain B residue 108 type sequence F description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 30) chain B residue 198 type sequence Y description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 31) chain B residue 228 type sequence D description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 32) chain B residue 230 type sequence G description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 33) chain B residue 231 type sequence T description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 34) chain B residue 232 type sequence T description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 35) chain B residue 235 type sequence R description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 36) chain B residue 328 type sequence S description BINDING SITE FOR CHAIN D OF INHIBITOR source : AC2 37) chain A residue 29-40 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141 38) chain A residue 42 type ACT_SITE sequence A description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 238 type ACT_SITE sequence K description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 42 type ACT_SITE sequence A description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 238 type ACT_SITE sequence K description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 75 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 228 type MOD_RES sequence D description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 234 type MOD_RES sequence L description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 248 type MOD_RES sequence I description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 249 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 256 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 228 type MOD_RES sequence D description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 234 type MOD_RES sequence L description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 248 type MOD_RES sequence I description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 249 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 256 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 75 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 102 type CARBOHYD sequence I description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 121 type CARBOHYD sequence L description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 172 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 303 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 60) chain B residue 102 type CARBOHYD sequence I description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 61) chain B residue 121 type CARBOHYD sequence L description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 172 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 303 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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