eF-site ID 3nex-AB PDB Code 3nex Chain A, B click to enlarge Title V30M mutant human transthyretin (TTR) complexed with GC-24 (V30M:GC-24) Classification TRANSPORT PROTEIN Compound Transthyretin Source Homo sapiens (Human) (TTHY_HUMAN) Sequence A:  CPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP B:  CPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKT SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP Description Functional site 1) chain A residue 44 type sequence F description BINDING SITE FOR RESIDUE GOL A 1 source : AC1 2) chain A residue 66 type sequence E description BINDING SITE FOR RESIDUE GOL A 1 source : AC1 3) chain A residue 99 type sequence D description BINDING SITE FOR RESIDUE GOL A 1 source : AC1 4) chain A residue 13 type sequence M description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 5) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 6) chain A residue 17 type sequence L description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 7) chain A residue 54 type sequence E description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 8) chain A residue 108 type sequence A description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 9) chain A residue 108 type sequence A description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 10) chain A residue 109 type sequence A description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 11) chain A residue 110 type sequence L description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 12) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 13) chain A residue 117 type sequence S description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 14) chain A residue 119 type sequence T description BINDING SITE FOR RESIDUE G24 A 126 source : AC2 15) chain B residue 44 type sequence F description BINDING SITE FOR RESIDUE GOL B 1 source : AC3 16) chain B residue 63 type sequence E description BINDING SITE FOR RESIDUE GOL B 1 source : AC3 17) chain B residue 66 type sequence E description BINDING SITE FOR RESIDUE GOL B 1 source : AC3 18) chain B residue 99 type sequence D description BINDING SITE FOR RESIDUE GOL B 1 source : AC3 19) chain B residue 100 type sequence S description BINDING SITE FOR RESIDUE GOL B 1 source : AC3 20) chain B residue 13 type sequence M description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 21) chain B residue 15 type sequence K description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 22) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 23) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 24) chain B residue 54 type sequence E description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 25) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 26) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 27) chain B residue 109 type sequence A description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 28) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 29) chain B residue 110 type sequence L description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 30) chain B residue 117 type sequence S description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 31) chain B residue 119 type sequence T description BINDING SITE FOR RESIDUE G24 B 126 source : AC4 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 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 41) 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 42) 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 43) 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 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 46) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769

Display surface Download Links