eF-site ID 4wns-AB PDB Code 4wns Chain A, B click to enlarge Title Crystal structure of Transthyretin complexed with pterostilbene 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 70 type sequence K description binding site for residue SO4 A 201 source : AC1 2) chain A residue 72 type sequence E description binding site for residue SO4 A 201 source : AC1 3) chain A residue 90 type sequence H description binding site for residue SO4 A 201 source : AC1 4) chain B residue 41 type sequence W description binding site for residue SO4 A 201 source : AC1 5) chain B residue 70 type sequence K description binding site for residue SO4 A 201 source : AC1 6) chain A residue 37 type sequence A description binding site for residue DMS A 202 source : AC2 7) chain A residue 38 type sequence D description binding site for residue DMS A 202 source : AC2 8) chain A residue 50 type sequence S description binding site for residue DMS A 202 source : AC2 9) chain A residue 51 type sequence E description binding site for residue DMS A 202 source : AC2 10) chain A residue 41 type sequence W description binding site for residue SO4 B 201 source : AC3 11) chain A residue 70 type sequence K description binding site for residue SO4 B 201 source : AC3 12) chain B residue 70 type sequence K description binding site for residue SO4 B 201 source : AC3 13) chain B residue 72 type sequence E description binding site for residue SO4 B 201 source : AC3 14) chain B residue 90 type sequence H description binding site for residue SO4 B 201 source : AC3 15) chain B residue 92 type sequence E description binding site for residue SO4 B 201 source : AC3 16) chain B residue 26 type sequence I description binding site for residue DMS B 202 source : AC4 17) chain B residue 27 type sequence N description binding site for residue DMS B 202 source : AC4 18) chain B residue 78 type sequence Y description binding site for residue DMS B 202 source : AC4 19) chain B residue 64 type sequence F description binding site for residue DMS B 203 source : AC5 20) chain B residue 98 type sequence N description binding site for residue DMS B 203 source : AC5 21) chain B residue 99 type sequence D description binding site for residue DMS B 203 source : AC5 22) chain B residue 102 type sequence P description binding site for residue DMS B 203 source : AC5 23) chain B residue 105 type sequence Y description binding site for residue DMS B 203 source : AC5 24) chain B residue 15 type sequence K description binding site for residue 3RL B 204 source : AC6 25) chain B residue 17 type sequence L description binding site for residue 3RL B 204 source : AC6 26) chain B residue 110 type sequence L description binding site for residue 3RL B 204 source : AC6 27) chain B residue 110 type sequence L description binding site for residue 3RL B 204 source : AC6 28) chain B residue 117 type sequence S description binding site for residue 3RL B 204 source : AC6 29) chain B residue 117 type sequence S description binding site for residue 3RL B 204 source : AC6 30) chain A residue 15-30 type prosite sequence KVLDAVRGSPAINVAV description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV source prosite : PS00768 31) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769 32) 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 33) 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 34) chain A residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 35) chain A residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 36) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 37) chain B residue 15 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 38) chain B residue 54 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 39) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT source Swiss-Prot : SWS_FT_FI1 40) 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 41) 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 42) 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 43) 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 44) chain A residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 45) 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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