eF-site ID 3ktm-ABCDEFGH PDB Code 3ktm Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) Classification CELL ADHESION, SIGNALING PROTEIN Compound Amyloid beta A4 protein Source Homo sapiens (Human) (A4_HUMAN) Sequence A:  LLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKE GILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKT HPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETH LHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCC PLAIEGRKLAAALEH B:  AGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDT KEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQC KTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCE THLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFV CCPLAIEGRKLAA C:  AGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDT KEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQC KTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCE THLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFV CCPLAIEGRKLAAA D:  LLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKE GILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKT HPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETH LHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCC PLAIEGRKLAAAL E:  AGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDT KEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQC KTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCE THLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFV CCPLAIEGRKLAAALEH F:  LLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKE GILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKT HPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETH LHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCC PLAIEGRKLAAALEH G:  LLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKE GILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKT HPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETH LHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCC PLAIEGRKLAAALE H:  AGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDT KEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQC KTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCE THLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFV CCPLAIEGRKLAAAL Description Functional site 1) chain A residue 83 type sequence T description BINDING SITE FOR RESIDUE BU4 A 1 source : AC1 2) chain A residue 84 type sequence N description BINDING SITE FOR RESIDUE BU4 A 1 source : AC1 3) chain A residue 173 type sequence P description BINDING SITE FOR RESIDUE BU4 A 1 source : AC1 4) chain A residue 174 type sequence C description BINDING SITE FOR RESIDUE BU4 A 1 source : AC1 5) chain A residue 175 type sequence G description BINDING SITE FOR RESIDUE BU4 A 1 source : AC1 6) chain A residue 176 type sequence I description BINDING SITE FOR RESIDUE BU4 A 1 source : AC1 7) chain B residue 188 type sequence P description BINDING SITE FOR RESIDUE BU4 B 7 source : AC2 8) chain B residue 189 type sequence L description BINDING SITE FOR RESIDUE BU4 B 7 source : AC2 9) chain B residue 190 type sequence A description BINDING SITE FOR RESIDUE BU4 B 7 source : AC2 10) chain G residue 194 type sequence R description BINDING SITE FOR RESIDUE BU4 B 7 source : AC2 11) chain B residue 88 type sequence A description BINDING SITE FOR RESIDUE SO4 B 2 source : AC3 12) chain B residue 89 type sequence N description BINDING SITE FOR RESIDUE SO4 B 2 source : AC3 13) chain B residue 116 type sequence R description BINDING SITE FOR RESIDUE SO4 B 2 source : AC3 14) chain H residue 194 type sequence R description BINDING SITE FOR RESIDUE SO4 B 2 source : AC3 15) chain B residue 90 type sequence Q description BINDING SITE FOR RESIDUE ACT B 208 source : AC4 16) chain B residue 151 type sequence H description BINDING SITE FOR RESIDUE ACT B 208 source : AC4 17) chain B residue 155 type sequence K description BINDING SITE FOR RESIDUE ACT B 208 source : AC4 18) chain A residue 194 type sequence R description BINDING SITE FOR RESIDUE BU4 C 5 source : AC5 19) chain C residue 189 type sequence L description BINDING SITE FOR RESIDUE BU4 C 5 source : AC5 20) chain C residue 190 type sequence A description BINDING SITE FOR RESIDUE BU4 C 5 source : AC5 21) chain C residue 89 type sequence N description BINDING SITE FOR RESIDUE SO4 C 3 source : AC6 22) chain C residue 116 type sequence R description BINDING SITE FOR RESIDUE SO4 C 3 source : AC6 23) chain E residue 194 type sequence R description BINDING SITE FOR RESIDUE SO4 C 3 source : AC6 24) chain C residue 90 type sequence Q description BINDING SITE FOR RESIDUE ACT C 8 source : AC7 25) chain C residue 151 type sequence H description BINDING SITE FOR RESIDUE ACT C 8 source : AC7 26) chain E residue 155 type sequence K description BINDING SITE FOR RESIDUE ACT C 8 source : AC7 27) chain D residue 83 type sequence T description BINDING SITE FOR RESIDUE BU4 D 2 source : AC8 28) chain D residue 84 type sequence N description BINDING SITE FOR RESIDUE BU4 D 2 source : AC8 29) chain D residue 173 type sequence P description BINDING SITE FOR RESIDUE BU4 D 2 source : AC8 30) chain D residue 174 type sequence C description BINDING SITE FOR RESIDUE BU4 D 2 source : AC8 31) chain D residue 175 type sequence G description BINDING SITE FOR RESIDUE BU4 D 2 source : AC8 32) chain A residue 180 type sequence R description BINDING SITE FOR RESIDUE SO4 D 5 source : AC9 33) chain D residue 140 type sequence R description BINDING SITE FOR RESIDUE SO4 D 5 source : AC9 34) chain E residue 189 type sequence L description BINDING SITE FOR RESIDUE BU4 E 6 source : BC1 35) chain E residue 190 type sequence A description BINDING SITE FOR RESIDUE BU4 E 6 source : BC1 36) chain F residue 194 type sequence R description BINDING SITE FOR RESIDUE BU4 E 6 source : BC1 37) chain C residue 194 type sequence R description BINDING SITE FOR RESIDUE SO4 E 4 source : BC2 38) chain E residue 88 type sequence A description BINDING SITE FOR RESIDUE SO4 E 4 source : BC2 39) chain E residue 89 type sequence N description BINDING SITE FOR RESIDUE SO4 E 4 source : BC2 40) chain E residue 116 type sequence R description BINDING SITE FOR RESIDUE SO4 E 4 source : BC2 41) chain E residue 90 type sequence Q description BINDING SITE FOR RESIDUE ACT E 9 source : BC3 42) chain E residue 151 type sequence H description BINDING SITE FOR RESIDUE ACT E 9 source : BC3 43) chain E residue 155 type sequence K description BINDING SITE FOR RESIDUE ACT E 9 source : BC3 44) chain F residue 175 type sequence G description BINDING SITE FOR RESIDUE BU4 F 4 source : BC4 45) chain F residue 176 type sequence I description BINDING SITE FOR RESIDUE BU4 F 4 source : BC4 46) chain G residue 173 type sequence P description BINDING SITE FOR RESIDUE BU4 G 3 source : BC5 47) chain G residue 174 type sequence C description BINDING SITE FOR RESIDUE BU4 G 3 source : BC5 48) chain G residue 175 type sequence G description BINDING SITE FOR RESIDUE BU4 G 3 source : BC5 49) chain G residue 176 type sequence I description BINDING SITE FOR RESIDUE BU4 G 3 source : BC5 50) chain D residue 194 type sequence R description BINDING SITE FOR RESIDUE BU4 H 8 source : BC6 51) chain H residue 189 type sequence L description BINDING SITE FOR RESIDUE BU4 H 8 source : BC6 52) chain H residue 190 type sequence A description BINDING SITE FOR RESIDUE BU4 H 8 source : BC6 53) chain B residue 194 type sequence R description BINDING SITE FOR RESIDUE SO4 H 1 source : BC7 54) chain H residue 88 type sequence A description BINDING SITE FOR RESIDUE SO4 H 1 source : BC7 55) chain H residue 89 type sequence N description BINDING SITE FOR RESIDUE SO4 H 1 source : BC7 56) chain H residue 116 type sequence R description BINDING SITE FOR RESIDUE SO4 H 1 source : BC7 57) chain H residue 90 type sequence Q description BINDING SITE FOR RESIDUE ACT H 6 source : BC8 58) chain H residue 151 type sequence H description BINDING SITE FOR RESIDUE ACT H 6 source : BC8 59) chain H residue 155 type sequence K description BINDING SITE FOR RESIDUE ACT H 6 source : BC8 60) chain A residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 63) chain D residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 64) chain E residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 65) chain F residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 66) chain G residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 67) chain H residue 96 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8158260 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 69) chain B residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 70) chain C residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 71) chain D residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 72) chain E residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 73) chain F residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 74) chain G residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 75) chain H residue 168 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 77) chain E residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 78) chain F residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 79) chain F residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 80) chain G residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 81) chain G residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 82) chain H residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 83) chain H residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 84) chain A residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 85) chain B residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 86) chain B residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 87) chain C residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 88) chain C residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 89) chain D residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 90) chain D residue 151 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 91) chain E residue 147 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU01217, ECO:0000269|PubMed:17239395, ECO:0000269|PubMed:25122912, ECO:0007744|PDB:2FK1 source Swiss-Prot : SWS_FT_FI2 92) chain A residue 181-188 type prosite sequence GVEFVCCP description APP_CUBD Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. GVEFVCCP source prosite : PS00319 93) chain A residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 94) chain D residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 95) chain D residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 96) chain D residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 97) chain E residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 98) chain E residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 99) chain E residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 100) chain F residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 101) chain F residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 102) chain F residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 103) chain G residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 104) chain A residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 105) chain G residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 106) chain G residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 107) chain H residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 108) chain H residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 109) chain H residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 110) chain A residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 111) chain B residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 112) chain B residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 113) chain B residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 114) chain C residue 183 type BINDING sequence E description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 115) chain C residue 186 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 116) chain C residue 187 type BINDING sequence C description BINDING => ECO:0000305|PubMed:8344894 source Swiss-Prot : SWS_FT_FI4 117) chain A residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 118) chain B residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 119) chain C residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 120) chain D residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 121) chain E residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 122) chain F residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 123) chain G residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5 124) chain H residue 170 type SITE sequence M description Required for Cu(2+) reduction => ECO:0000255|PROSITE-ProRule:PRU01217 source Swiss-Prot : SWS_FT_FI5

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