eF-site ID 2vkm-D PDB Code 2vkm Chain D click to enlarge Title Crystal structure of GRL-8234 bound to BACE (Beta-secretase) Classification HYDROLASE Compound BETA-SECRETASE 1 Source Homo sapiens (Human) (BACE1_HUMAN) Sequence D:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN Description Functional site 1) chain D residue 11 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 2) chain D residue 12 type sequence Q description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 3) chain D residue 13 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 4) chain D residue 30 type sequence L description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 5) chain D residue 32 type sequence D description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 6) chain D residue 34 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 7) chain D residue 35 type sequence S description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 8) chain D residue 69 type sequence V description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 9) chain D residue 70 type sequence P description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 10) chain D residue 71 type sequence Y description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 11) chain D residue 72 type sequence T description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 12) chain D residue 73 type sequence Q description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 13) chain D residue 108 type sequence F description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 14) chain D residue 110 type sequence I description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 15) chain D residue 115 type sequence W description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 16) chain D residue 228 type sequence D description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 17) chain D residue 229 type sequence S description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 18) chain D residue 230 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 19) chain D residue 231 type sequence T description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 20) chain D residue 232 type sequence T description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 21) chain D residue 233 type sequence N description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 22) chain D residue 235 type sequence R description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 23) chain D residue 307 type sequence R description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 24) chain D residue 325 type sequence S description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 25) chain D residue 335 type sequence A description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 26) chain D residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 27) chain D residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 28) chain D residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 29) chain D residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 30) chain D residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 65 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 33) chain D residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 34) chain D residue 218 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 35) chain D residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 36) chain D residue 238 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 37) chain D residue 239 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 38) chain D residue 246 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2

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