eF-site ID 2zjj-A PDB Code 2zjj Chain A click to enlarge Title Crystal structure of the human BACE1 catalytic domain in complex with 4-(4-fluoro-benzyl)-piperazine-2-carboxylic acid (2-mercapto-ethyl)-amide Classification HYDROLASE Compound Beta-secretase 1 Source Homo sapiens (Human) (BACE1_HUMAN) Sequence A:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGAW AGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEIN GQDLKMDCKEYNYDKSIVDSGCTNLRLPKKVFEAAVKSIK AASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMG EVTNQSFRITILPQQYLRPVEDDCYKFAISQSSTGTVMGA VIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFV TLDMEDCGYN Description Functional site 1) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 2) chain A residue 12 type sequence Q description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 3) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 4) chain A residue 30 type sequence L description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 5) chain A residue 71 type sequence Y description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 6) chain A residue 72 type sequence T description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 7) chain A residue 73 type sequence Q description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 8) chain A residue 108 type sequence F description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 9) chain A residue 230 type sequence G description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 10) chain A residue 231 type sequence C description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 11) chain A residue 232 type sequence T description BINDING SITE FOR RESIDUE F1J A 449 source : AC1 12) chain A residue 29-40 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141 13) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) chain A residue 246 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 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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