eF-site ID 2fdp-C PDB Code 2fdp Chain 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 C:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA SVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLM GEVTNQSFRITILPQQYLRPVEDSQDDCYKFAISQSSTGT VMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVE GPFVTLDMEDCGYN Description Functional site 1) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 2) chain C residue 12 type sequence Q description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 3) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 4) chain C residue 32 type sequence D description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 5) chain C residue 34 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 6) chain C residue 35 type sequence S description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 7) chain C residue 70 type sequence P description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 8) chain C residue 71 type sequence Y description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 9) chain C residue 72 type sequence T description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 10) chain C residue 73 type sequence Q description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 11) chain C residue 108 type sequence F description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 12) chain C residue 126 type sequence I description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 13) chain C residue 128 type sequence R description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 14) chain C residue 228 type sequence D description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 15) chain C residue 230 type sequence G description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 16) chain C residue 231 type sequence T description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 17) chain C residue 232 type sequence T description BINDING SITE FOR RESIDUE FRP C 386 source : AC3 18) chain C residue 80 type ACT_SITE sequence L description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 276 type ACT_SITE sequence P description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 113 type MOD_RES sequence S description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 262 type MOD_RES sequence W description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 266 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 272 type MOD_RES sequence A description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 286 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 287 type MOD_RES sequence L description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 26) chain C residue 294 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 210 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 341 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 140 type CARBOHYD sequence L description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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