eF-site ID 2wf4-A PDB Code 2wf4 Chain A click to enlarge Title Human BACE-1 in complex with 6-ethyl-1-methyl-N-((1S)-2-oxo-1-(phenylmethyl)-3-(tetrahydro-2H-pyran-4-ylamino)propyl)-1,3,4,6- tetrahydro(1,2)thiazepino(5,4,3-cd)indole-8-carboxamide 2,2-dioxide Classification HYDROLASE Compound BETA-SECRETASE 1 Source (BACE1_HUMAN) Sequence A:  EMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAV GAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGEL GTDLVSIPHGPQVTVRANIAAITESDKFFIQGSNWEGILG LAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCSVGGS MIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDL KMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASS TEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTQ QSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVM GAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGP FVTLDMEDCGYNI Description (1)  BETA-SECRETASE 1 (E.C.3.4.23.46) Functional site 1) chain A residue 72 type sequence G description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 2) chain A residue 73 type sequence Q description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 3) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 4) chain A residue 95 type sequence G description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 5) chain A residue 132 type sequence Y description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 6) chain A residue 133 type sequence T description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 7) chain A residue 134 type sequence Q description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 8) chain A residue 169 type sequence F description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 9) chain A residue 259 type sequence Y description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 10) chain A residue 287 type sequence I description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 11) chain A residue 289 type sequence D description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 12) chain A residue 291 type sequence G description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 13) chain A residue 292 type sequence T description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 14) chain A residue 293 type sequence T description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 15) chain A residue 294 type sequence N description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 16) chain A residue 296 type sequence R description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 17) chain A residue 386 type sequence S description BINDING SITE FOR RESIDUE ZY4 A 2000 source : AC1 18) chain A residue 93 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 289 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 126 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 275 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 279 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 285 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 299 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 25) 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 26) chain A residue 307 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 153 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 172 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 354 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 90-101 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141

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