eF-site ID 2fdp-B PDB Code 2fdp Chain B 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 B:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA SVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEI NGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSI KAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLM GEVTNQSFRITILPQQYLRPVDCYKFAISQSSTGTVMGAV IMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVT LDMEDCGYN Description Functional site 1) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 2) chain B residue 12 type sequence Q description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 3) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 4) chain B residue 32 type sequence D description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 5) chain B residue 34 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 6) chain B residue 35 type sequence S description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 7) chain B residue 70 type sequence P description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 8) chain B residue 71 type sequence Y description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 9) chain B residue 72 type sequence T description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 10) chain B residue 73 type sequence Q description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 11) chain B residue 108 type sequence F description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 12) chain B residue 126 type sequence I description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 13) chain B residue 128 type sequence R description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 14) chain B residue 228 type sequence D description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 15) chain B residue 230 type sequence G description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 16) chain B residue 231 type sequence T description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 17) chain B residue 232 type sequence T description BINDING SITE FOR RESIDUE FRP B 386 source : AC2 18) chain B residue 80 type ACT_SITE sequence L description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 276 type ACT_SITE sequence P description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 266 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 272 type MOD_RES sequence A description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 286 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 287 type MOD_RES sequence L description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 294 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 113 type MOD_RES sequence S description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 262 type MOD_RES sequence W description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 140 type CARBOHYD sequence L description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 210 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 341 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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