eF-site ID 2fdp-ABC PDB Code 2fdp Chain A, B, C click to enlarge Title Crystal structure of beta-secretase complexed with an amino-ethylene inhibitor Classification HYDROLASE Compound Beta-secretase 1 Source Homo sapiens (Human) (BACE1_HUMAN) Sequence A:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA SVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLM GEVTNQSFRITILPQQYLRPVESQDDCYKFAISQSSTGTV MGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEG PFVTLDMEDCGYN B:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA SVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLM GEVTNQSFRITILPQQYLRPVDCYKFAISQSSTGTVMGAV IMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVT LDMEDCGYN C:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA SVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLM GEVTNQSFRITILPQQYLRPVEDSQDDCYKFAISQSSTGT VMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVE GPFVTLDMEDCGYN Description Functional site 1) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 2) chain A residue 12 type sequence Q description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 3) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 4) chain A residue 32 type sequence D description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 5) chain A residue 34 type sequence G description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 6) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 7) chain A residue 70 type sequence P description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 8) chain A residue 71 type sequence Y description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 9) chain A residue 72 type sequence T description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 10) chain A residue 73 type sequence Q description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 11) chain A residue 108 type sequence F description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 12) chain A residue 126 type sequence I description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 13) chain A residue 128 type sequence R description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 14) chain A residue 228 type sequence D description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 15) chain A residue 230 type sequence G description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 16) chain A residue 231 type sequence T description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 17) chain A residue 232 type sequence T description BINDING SITE FOR RESIDUE FRP A 386 source : AC1 18) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 19) chain B residue 12 type sequence Q description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 20) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 21) chain B residue 32 type sequence D description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 22) chain B residue 34 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 23) chain B residue 35 type sequence S description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 24) chain B residue 70 type sequence P description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 25) chain B residue 71 type sequence Y description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 26) chain B residue 72 type sequence T description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 27) chain B residue 73 type sequence Q description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 28) chain B residue 108 type sequence F description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 29) chain B residue 126 type sequence I description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 30) chain B residue 128 type sequence R description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 31) chain B residue 228 type sequence D description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 32) chain B residue 230 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 33) chain B residue 231 type sequence T description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 34) chain B residue 232 type sequence T description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 35) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 36) chain C residue 12 type sequence Q description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 37) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 38) chain C residue 32 type sequence D description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 39) chain C residue 34 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 40) chain C residue 35 type sequence S description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 41) chain C residue 70 type sequence P description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 42) chain C residue 71 type sequence Y description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 43) chain C residue 72 type sequence T description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 44) chain C residue 73 type sequence Q description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 45) chain C residue 108 type sequence F description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 46) chain C residue 126 type sequence I description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 47) chain C residue 128 type sequence R description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 48) chain C residue 228 type sequence D description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 49) chain C residue 230 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 50) chain C residue 231 type sequence T description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 51) chain C residue 232 type sequence T description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 52) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 65 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 59) chain B residue 218 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 60) 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 61) chain B residue 238 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 239 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 63) chain B residue 246 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 64) chain C residue 65 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 65) chain C residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 66) chain C residue 218 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 67) chain C residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 68) chain C residue 238 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 239 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 246 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 72) chain A residue 218 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 73) 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 74) chain A residue 238 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 75) chain A residue 239 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 246 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 77) chain B residue 65 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 78) chain B residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 79) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 80) chain C residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 81) chain C residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 84) chain B residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 85) chain B residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 86) chain B residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 87) chain C residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 88) chain A residue 29-40 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141

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