eF-site ID 2vkm-A PDB Code 2vkm Chain A click to enlarge Title Crystal structure of GRL-8234 bound to BACE (Beta-secretase) Classification HYDROLASE Compound BETA-SECRETASE 1 Source null (BACE1_HUMAN) Sequence A:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN Description Functional site 1) chain A residue 12 type sequence Q description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 2) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 3) chain A residue 30 type sequence L description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 4) chain A residue 32 type sequence D description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 5) chain A residue 34 type sequence G description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 6) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 7) chain A residue 70 type sequence P description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 8) chain A residue 71 type sequence Y description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 9) chain A residue 72 type sequence T description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 10) chain A residue 73 type sequence Q description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 11) chain A residue 108 type sequence F description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 12) chain A residue 115 type sequence W description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 13) chain A residue 126 type sequence I description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 14) chain A residue 228 type sequence D description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 15) chain A residue 229 type sequence S description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 16) chain A residue 230 type sequence G description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 17) chain A residue 231 type sequence T description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 18) chain A residue 232 type sequence T description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 19) chain A residue 233 type sequence N description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 20) chain A residue 235 type sequence R description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 21) chain A residue 325 type sequence S description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 22) chain A residue 335 type sequence A description BINDING SITE FOR RESIDUE BSD A1386 source : AC1 23) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 29-40 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141

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