eF-site ID 4wo0-AB PDB Code 4wo0 Chain A, B click to enlarge Title Crystal structure of transthyretin in complex with apigenin Classification TRANSPORT PROTEIN Compound Transthyretin Source Homo sapiens (Human) (TTHY_HUMAN) Sequence A:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN B:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN Description Functional site 1) chain A residue 15 type sequence K description binding site for residue AGI A 201 source : AC1 2) chain A residue 15 type sequence K description binding site for residue AGI A 201 source : AC1 3) chain A residue 17 type sequence L description binding site for residue AGI A 201 source : AC1 4) chain A residue 17 type sequence L description binding site for residue AGI A 201 source : AC1 5) chain A residue 108 type sequence A description binding site for residue AGI A 201 source : AC1 6) chain A residue 110 type sequence L description binding site for residue AGI A 201 source : AC1 7) chain A residue 117 type sequence S description binding site for residue AGI A 201 source : AC1 8) chain A residue 117 type sequence S description binding site for residue AGI A 201 source : AC1 9) chain A residue 118 type sequence T description binding site for residue AGI A 201 source : AC1 10) chain A residue 119 type sequence T description binding site for residue AGI A 201 source : AC1 11) chain A residue 119 type sequence T description binding site for residue AGI A 201 source : AC1 12) chain B residue 15 type sequence K description binding site for residue AGI B 201 source : AC2 13) chain B residue 15 type sequence K description binding site for residue AGI B 201 source : AC2 14) chain B residue 17 type sequence L description binding site for residue AGI B 201 source : AC2 15) chain B residue 108 type sequence A description binding site for residue AGI B 201 source : AC2 16) chain B residue 110 type sequence L description binding site for residue AGI B 201 source : AC2 17) chain B residue 117 type sequence S description binding site for residue AGI B 201 source : AC2 18) chain B residue 117 type sequence S description binding site for residue AGI B 201 source : AC2 19) chain B residue 118 type sequence T description binding site for residue AGI B 201 source : AC2 20) chain B residue 119 type sequence T description binding site for residue AGI B 201 source : AC2 21) chain B residue 119 type sequence T description binding site for residue AGI B 201 source : AC2 22) chain A residue 15-30 type prosite sequence KVLDAVRGSPAINVAV description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV source prosite : PS00768 23) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) chain A residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 33) chain B residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 34) chain B residue 117 type BINDING sequence S 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 A residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 37) chain A residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1

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