eF-site ID 2vkm-ABCD PDB Code 2vkm Chain A, B, C, 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 A:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN B:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN C:  GSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSS NFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKW EGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWE GILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCG AGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRRE WYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRL PKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTP WNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQ DDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAV SACHVHDEFRTAAVEGPFVTLDMEDCGYN D:  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 B residue 12 type sequence Q description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 24) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 25) chain B residue 30 type sequence L description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 26) chain B residue 32 type sequence D description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 27) chain B residue 34 type sequence G description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 28) chain B residue 35 type sequence S description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 29) chain B residue 69 type sequence V description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 30) chain B residue 71 type sequence Y description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 31) chain B residue 72 type sequence T description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 32) chain B residue 73 type sequence Q description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 33) chain B residue 108 type sequence F description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 34) chain B residue 115 type sequence W description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 35) chain B residue 228 type sequence D description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 36) chain B residue 229 type sequence S description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 37) chain B residue 230 type sequence G description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 38) chain B residue 231 type sequence T description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 39) chain B residue 232 type sequence T description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 40) chain B residue 233 type sequence N description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 41) chain B residue 235 type sequence R description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 42) chain B residue 325 type sequence S description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 43) chain B residue 335 type sequence A description BINDING SITE FOR RESIDUE BSD B1386 source : AC2 44) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 45) chain C residue 12 type sequence Q description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 46) chain C residue 13 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 47) chain C residue 32 type sequence D description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 48) chain C residue 34 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 49) chain C residue 35 type sequence S description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 50) chain C residue 69 type sequence V description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 51) chain C residue 70 type sequence P description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 52) chain C residue 71 type sequence Y description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 53) chain C residue 72 type sequence T description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 54) chain C residue 73 type sequence Q description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 55) chain C residue 108 type sequence F description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 56) chain C residue 110 type sequence I description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 57) chain C residue 115 type sequence W description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 58) chain C residue 118 type sequence I description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 59) chain C residue 228 type sequence D description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 60) chain C residue 229 type sequence S description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 61) chain C residue 230 type sequence G description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 62) chain C residue 231 type sequence T description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 63) chain C residue 232 type sequence T description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 64) chain C residue 233 type sequence N description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 65) chain C residue 235 type sequence R description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 66) chain C residue 307 type sequence R description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 67) chain C residue 325 type sequence S description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 68) chain C residue 335 type sequence A description BINDING SITE FOR RESIDUE BSD C1386 source : AC3 69) chain D residue 11 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 70) chain D residue 12 type sequence Q description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 71) chain D residue 13 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 72) chain D residue 30 type sequence L description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 73) chain D residue 32 type sequence D description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 74) chain D residue 34 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 75) chain D residue 35 type sequence S description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 76) chain D residue 69 type sequence V description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 77) chain D residue 70 type sequence P description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 78) chain D residue 71 type sequence Y description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 79) chain D residue 72 type sequence T description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 80) chain D residue 73 type sequence Q description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 81) chain D residue 108 type sequence F description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 82) chain D residue 110 type sequence I description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 83) chain D residue 115 type sequence W description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 84) chain D residue 228 type sequence D description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 85) chain D residue 229 type sequence S description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 86) chain D residue 230 type sequence G description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 87) chain D residue 231 type sequence T description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 88) chain D residue 232 type sequence T description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 89) chain D residue 233 type sequence N description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 90) chain D residue 235 type sequence R description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 91) chain D residue 307 type sequence R description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 92) chain D residue 325 type sequence S description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 93) chain D residue 335 type sequence A description BINDING SITE FOR RESIDUE BSD D1386 source : AC4 94) chain A residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 95) chain C residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 96) chain C residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 97) chain C residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 98) chain D residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 99) chain D residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 100) chain D residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 101) chain D residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 102) chain A residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 103) chain A residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 104) chain A residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 105) chain B residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 106) chain B residue 111 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 107) chain B residue 162 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 108) chain B residue 293 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 109) chain C residue 92 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 110) chain A residue 29-40 type prosite sequence ILVDTGSSNFAV description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV source prosite : PS00141 111) chain A residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 112) chain A residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 113) chain B residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 114) chain B residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 115) chain C residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 116) chain C residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 117) chain D residue 32 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 118) chain D residue 228 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094 source Swiss-Prot : SWS_FT_FI1 119) 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 120) chain B residue 218 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 121) chain B residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 122) chain B residue 238 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 123) chain B residue 239 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 124) chain B residue 246 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 125) 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 126) 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 127) 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 128) 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 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) 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 136) 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 137) 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 138) 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 139) 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 140) 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 141) 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 142) 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 143) 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 144) 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 145) chain B residue 65 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241 source Swiss-Prot : SWS_FT_FI2 146) chain B residue 214 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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