eF-site ID 2vkm-C PDB Code 2vkm Chain C 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 C:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN Description Functional site 1) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 2) chain C residue 12 type sequence Q description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 3) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 4) chain C residue 32 type sequence D description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 5) chain C residue 34 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 6) chain C residue 35 type sequence S description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 7) chain C residue 69 type sequence V description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 8) chain C residue 70 type sequence P description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 9) chain C residue 71 type sequence Y description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 10) chain C residue 72 type sequence T description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 11) chain C residue 73 type sequence Q description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 12) chain C residue 108 type sequence F description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 13) chain C residue 110 type sequence I description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 14) chain C residue 115 type sequence W description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 15) chain C residue 118 type sequence I description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 16) chain C residue 228 type sequence D description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 17) chain C residue 229 type sequence S description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 18) chain C residue 230 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 19) chain C residue 231 type sequence T description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 20) chain C residue 232 type sequence T description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 21) chain C residue 233 type sequence N description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 22) chain C residue 235 type sequence R description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 23) chain C residue 307 type sequence R description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 24) chain C residue 325 type sequence S description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 25) chain C residue 335 type sequence A description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 26) chain C residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 27) chain C residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 30) chain C residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 32) chain C 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 C 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 C 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 C 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 C 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 C 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 C residue 246 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links