eF-site ID 5akt-AB PDB Code 5akt Chain A, B click to enlarge Title Transthyretin binding heterogeneity and anti-amyloidogenic activity of natural polyphenols and their metabolites: resveratrol-4'-O- glucuronide Classification TRANSPORT PROTEIN Compound TRANSTHYRETIN Source (TTHY_HUMAN) Sequence A:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP B:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN Description Functional site 1) chain A residue 35 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1126 source : AC1 2) chain A residue 41 type sequence W description BINDING SITE FOR RESIDUE SO4 A 1126 source : AC1 3) chain B residue 72 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1126 source : AC1 4) chain B residue 90 type sequence H description BINDING SITE FOR RESIDUE SO4 A 1126 source : AC1 5) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1127 source : AC2 6) chain A residue 90 type sequence H description BINDING SITE FOR RESIDUE SO4 A 1127 source : AC2 7) chain A residue 92 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1127 source : AC2 8) chain B residue 35 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1127 source : AC2 9) chain B residue 41 type sequence W description BINDING SITE FOR RESIDUE SO4 A 1127 source : AC2 10) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 11) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 12) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 13) chain B residue 54 type sequence E description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 14) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 15) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 16) chain B residue 117 type sequence S description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 17) chain B residue 117 type sequence S description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 18) chain B residue 118 type sequence T description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 19) chain B residue 119 type sequence T description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 20) chain B residue 119 type sequence T description BINDING SITE FOR RESIDUE R4G B 1128 source : AC3 21) chain A residue 13 type sequence M description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 22) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 23) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 24) chain A residue 17 type sequence L description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 25) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 26) chain A residue 54 type sequence E description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 27) chain A residue 54 type sequence E description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 28) chain A residue 110 type sequence L description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 29) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 30) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE R4G A 1128 source : AC4 31) chain A residue 15-30 type prosite sequence KVLDAVRGSPAINVAV description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV source prosite : PS00768 32) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769 33) chain A residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 34) chain A residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 35) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 36) chain B residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 37) chain B residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 38) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 39) chain A residue 98 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 98 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 10 type MOD_RES sequence C description Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E source Swiss-Prot : SWS_FT_FI2 42) chain B residue 10 type MOD_RES sequence C description Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E source Swiss-Prot : SWS_FT_FI2 43) chain A residue 42 type MOD_RES sequence E description 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 42 type MOD_RES sequence E description 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 46) chain B residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4

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