eF-site ID 2qu2-A PDB Code 2qu2 Chain A click to enlarge Title BACE1 with Compound 1 Classification HYDROLASE Compound Beta-secretase 1 Source Homo sapiens (Human) (BACE1_HUMAN) Sequence A:  SFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSN FAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWE GELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEG ILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGA SEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVII VRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEA AVKSIKAASSTEKFPDGFWLGEQLVCWAGTTPWNIFPVIS LYLMGEVTNQSFRITILPQQYLRPVDCYKFAISQSSTGTV MGAVIMEGFYVVFDRARKRIGFAVSACHDEFRTAAVEGPF VDCG Description (1)  Beta-secretase 1 (E.C.3.4.23.46) Functional site 1) chain A residue 94 type sequence D description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 2) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 3) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 4) chain A residue 170 type sequence F description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 5) chain A residue 177 type sequence W description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 6) chain A residue 180 type sequence I description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 7) chain A residue 190 type sequence R description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 8) chain A residue 290 type sequence D description BINDING SITE FOR RESIDUE 251 A 1 source : AC1 9) chain A residue 91-102 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141 10) chain A residue 94 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 290 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 280 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 286 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 300 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 301 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 308 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 154 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 173 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 355 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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