eF-site ID 1e4h-AB PDB Code 1e4h Chain A, B click to enlarge Title Structure of human transthyretin complexed with bromophenols: a new mode of binding Classification TRANSPORT PROTEIN Compound TRANSTHYRETIN Source ORGANISM_COMMON: HUMAN; ORGANISM_SCIENTIFIC: HOMO SAPIENS; Sequence A:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP B:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP Description Functional site 1) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 2) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 3) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 4) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 5) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 6) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 7) chain B residue 119 type sequence T description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 8) chain B residue 119 type sequence T description BINDING SITE FOR RESIDUE PBR A 998 source : AC1 9) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE PBR B 999 source : AC2 10) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE PBR B 999 source : AC2 11) chain A residue 119 type sequence T description BINDING SITE FOR RESIDUE PBR B 999 source : AC2 12) chain A residue 119 type sequence T description BINDING SITE FOR RESIDUE PBR B 999 source : AC2 13) chain A residue 41 type sequence W description BINDING SITE FOR RESIDUE GOL A 990 source : AC3 14) chain A residue 70 type sequence K description BINDING SITE FOR RESIDUE GOL A 990 source : AC3 15) chain A residue 72 type sequence E description BINDING SITE FOR RESIDUE GOL A 990 source : AC3 16) chain A residue 110 type sequence L description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 17) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 18) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 19) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 20) chain B residue 111 type sequence L description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 21) chain B residue 112 type sequence S description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 22) chain B residue 115 type sequence S description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 23) chain B residue 116 type sequence Y description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 24) chain B residue 117 type sequence S description BINDING SITE FOR RESIDUE GOL B 990 source : AC4 25) chain A residue 15-30 type prosite sequence KVLDAVRGSPAINVAV description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV source prosite : PS00768 26) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) chain A residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 36) chain A residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 37) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 38) chain B residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 39) chain B residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 40) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1

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