eF-site ID 3buf-A PDB Code 3buf Chain A click to enlarge Title BACE-1 complexed with compound 2 Classification HYDROLASE Compound Beta-secretase 1 Source Homo sapiens (Human) (BACE1_HUMAN) Sequence A:  RGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGS SNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGK WEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNW EGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLC GSVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVE INGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVAS IKAASSFPDGFWLGEQLVCWQAWNIFPVISLYLMGEVTNQ SFRITILPQQYLRPVDCYKFAISQSSTGTVMGAVIMEGFY VVFDRARKRIGFAVSACHRTAAVEGPFVTLDMEDCGYNI Description Functional site 1) chain A residue 32 type sequence D description BINDING SITE FOR RESIDUE AEG A 394 source : AC1 2) chain A residue 107 type sequence K description BINDING SITE FOR RESIDUE AEG A 394 source : AC1 3) chain A residue 108 type sequence F description BINDING SITE FOR RESIDUE AEG A 394 source : AC1 4) chain A residue 110 type sequence I description BINDING SITE FOR RESIDUE AEG A 394 source : AC1 5) chain A residue 230 type sequence G description BINDING SITE FOR RESIDUE AEG A 394 source : AC1 6) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 8) 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 9) 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 10) 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 11) 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 12) 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 13) 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 14) chain A residue 246 type MOD_RES sequence A description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 18) 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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