eF-site ID 1tyr-AB PDB Code 1tyr Chain A, B click to enlarge Title TRANSTHYRETIN COMPLEX WITH RETINOIC ACID Classification RETINOL-BINDING Compound TRANSTHYRETIN Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDT WEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTA VVTNPKE B:  GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDT WEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTA VVTNPKE Description (1)  TRANSTHYRETIN, RETINOIC ACID Functional site 1) chain A residue 15 type sequence K description source : A1 2) chain A residue 16 type sequence V description source : A1 3) chain A residue 17 type sequence L description source : A1 4) chain A residue 106 type sequence T description source : A1 5) chain A residue 107 type sequence I description source : A1 6) chain A residue 108 type sequence A description source : A1 7) chain A residue 109 type sequence A description source : A1 8) chain A residue 110 type sequence L description source : A1 9) chain A residue 117 type sequence S description source : A1 10) chain A residue 118 type sequence T description source : A1 11) chain A residue 119 type sequence T description source : A1 12) chain A residue 120 type sequence A description source : A1 13) chain A residue 121 type sequence V description source : A1 14) chain B residue 15 type sequence K description source : B1 15) chain B residue 16 type sequence V description source : B1 16) chain B residue 17 type sequence L description source : B1 17) chain B residue 106 type sequence T description source : B1 18) chain B residue 107 type sequence I description source : B1 19) chain B residue 108 type sequence A description source : B1 20) chain B residue 109 type sequence A description source : B1 21) chain B residue 110 type sequence L description source : B1 22) chain B residue 117 type sequence S description source : B1 23) chain B residue 118 type sequence T description source : B1 24) chain B residue 119 type sequence T description source : B1 25) chain B residue 120 type sequence A description source : B1 26) chain B residue 121 type sequence V description source : B1 27) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 28) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 29) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 30) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 31) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 32) chain B residue 117 type sequence S description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 33) chain B residue 119 type sequence T description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 34) chain B residue 121 type sequence V description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 35) chain B residue 127 type sequence E description BINDING SITE FOR RESIDUE 9CR B 130 source : AC1 36) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 37) chain A residue 17 type sequence L description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 38) chain A residue 17 type sequence L description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 39) chain A residue 106 type sequence T description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 40) chain A residue 108 type sequence A description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 41) chain A residue 108 type sequence A description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 42) chain A residue 109 type sequence A description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 43) chain A residue 110 type sequence L description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 44) chain A residue 110 type sequence L description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 45) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 46) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 47) chain A residue 119 type sequence T description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 48) chain A residue 121 type sequence V description BINDING SITE FOR RESIDUE 9CR A 131 source : AC2 49) chain A residue 15-30 type prosite sequence KVLDAVRGSPAINVAV description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV source prosite : PS00768 50) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769 51) 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 52) 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 53) chain A residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 54) chain A residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 55) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 56) chain B residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 57) chain B residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 58) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 59) 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 60) 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 61) 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 62) 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 63) chain A residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 64) 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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