eF-site ID 2wf1-A PDB Code 2wf1 Chain A click to enlarge Title Human BACE-1 in complex with 7-ethyl-N-((1S,2R)-2-hydroxy-3-(((3-(methyloxy)phenyl(methyl)amino)-1-(phenylmethyl)propyl)-1-methyl-3,4- dihydro-1H-(1,2,5)thiadiazepino(3,4,5-hi)indole-9-carboxamide 2,2- dioxide Classification HYDROLASE Compound BETA-SECRETASE 1 Source (BACE1_HUMAN) Sequence A:  EMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAV GAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGEL GTDLVSIPHGPQVTVRANIAAITESDKFFIQGSNWEGILG LAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGASVG GSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQ DLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAA SSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEV TQQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGT VMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVE GPFVTLDMEDCGYNI 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 ZY1 A 2000 source : AC1 2) chain A residue 73 type sequence Q description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 3) chain A residue 74 type sequence G description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 4) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 5) chain A residue 95 type sequence G description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 6) chain A residue 96 type sequence S description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 7) chain A residue 131 type sequence P description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 8) chain A residue 132 type sequence Y description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 9) chain A residue 133 type sequence T description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 10) chain A residue 134 type sequence Q description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 11) chain A residue 169 type sequence F description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 12) chain A residue 179 type sequence I description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 13) chain A residue 289 type sequence D description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 14) chain A residue 291 type sequence G description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 15) chain A residue 292 type sequence T description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 16) chain A residue 293 type sequence T description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 17) chain A residue 294 type sequence N description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 18) chain A residue 296 type sequence R description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 19) chain A residue 386 type sequence S description BINDING SITE FOR RESIDUE ZY1 A 2000 source : AC1 20) chain A residue 93 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 289 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) chain A residue 153 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 172 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 354 type CARBOHYD sequence Q description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 90-101 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141

Display surface Download Links