eF-site ID 3bsz-ABCDEFHLMN PDB Code 3bsz Chain A, B, C, D, E, F, H, L, M, N click to enlarge Title Crystal structure of the transthyretin-retinol binding protein-Fab complex Classification TRANSPORT PROTEIN/IMMUNE SYSTEM Compound Transthyretin Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  ESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFAS GKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISP FHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP B:  ESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFAS GKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISP FHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP C:  ESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFAS GKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISP FHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP D:  ESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFAS GKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISP FHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP E:  ERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDN IVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDT EDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSC RLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELC LARQYRLIVHNGYC F:  ERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDN IVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDT EDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSC RLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELC LARQYRLIVHNGYC H:  DVQLQESGTVLARPGASVKMSCKASGYSFTSYWMHWIKQR PGQGLEWIGGVYPGDSHTSYNQKFKGKAKLTAVTSASTAY MELSSLTNEDSAVYYCTRSGFDYGNEDWGQGTTLTVSSAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWN SGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTC NVAHPASSTKVDKKI L:  DIVLTQSPSSLAVSLGQRATISCRASESVDSYGNSFMHWY QQKPGQPPKLLIYRASNLESGIPARFSGSGSRTDFTLTIN PVEADDVATYYCQQSNEDPYTFGGGTKLEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQ NGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEA THKTSTSPIVKSFNR M:  DIVLTQSPSSLAVSLGQRATISCRASESVDSYGNSFMHWY QQKPGQPPKLLIYRASNLESGIPARFSGSGSRTDFTLTIN PVEADDVATYYCQQSNEDPYTFGGGTKLEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQ NGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEA THKTSTSPIVKSFNR N:  DVQLQESGTVLARPGASVKMSCKASGYSFTSYWMHWIKQR PGQGLEWIGGVYPGDSHTSYNQKFKGKAKLTAVTSASTAY MELSSLTNEDSAVYYCTRSGFDYGNEDWGQGTTLTVSSAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWN SGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTC NVAHPASSTKVDKKI Description Functional site 1) chain B residue 83 type sequence G description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 2) chain E residue 36 type sequence F description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 3) chain E residue 37 type sequence L description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 4) chain E residue 73 type sequence M description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 5) chain E residue 88 type sequence M description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 6) chain E residue 97 type sequence L description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 7) chain E residue 98 type sequence Q description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 8) chain E residue 104 type sequence H description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 9) chain E residue 135 type sequence F description BINDING SITE FOR RESIDUE RTL E 177 source : AC1 10) chain D residue 83 type sequence G description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 11) chain F residue 36 type sequence F description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 12) chain F residue 37 type sequence L description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 13) chain F residue 73 type sequence M description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 14) chain F residue 88 type sequence M description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 15) chain F residue 98 type sequence Q description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 16) chain F residue 104 type sequence H description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 17) chain F residue 135 type sequence F description BINDING SITE FOR RESIDUE RTL F 178 source : AC2 18) chain E residue 98 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 15 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 54 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 22) chain F residue 98 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 15 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 54 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 27) chain C residue 15 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 28) chain C residue 54 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P27485 source Swiss-Prot : SWS_FT_FI1 30) chain E residue 121 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724 source Swiss-Prot : SWS_FT_FI2 31) chain F residue 121 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724 source Swiss-Prot : SWS_FT_FI2 32) chain C residue 10 type MOD_RES sequence C description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724 source Swiss-Prot : SWS_FT_FI2 33) chain D residue 10 type MOD_RES sequence C description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724 source Swiss-Prot : SWS_FT_FI2 34) 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 35) 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 36) chain C 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 37) chain D 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 38) 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 39) 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 40) chain C 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 D 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 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 43) chain B residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 44) chain C residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 45) chain D residue 52 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02767 source Swiss-Prot : SWS_FT_FI4 46) chain L residue 196-202 type prosite sequence YTCEATH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH source prosite : PS00290 47) chain E residue 14-27 type prosite sequence NFDKARFSGTWYAM description LIPOCALIN Lipocalin signature. NFDkaRFSGTWYAM source prosite : PS00213 48) chain A residue 15-30 type prosite sequence KVLDAVRGSPAINVAV description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV source prosite : PS00768 49) chain A residue 105-117 type prosite sequence YTIAALLSPYSYS description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS source prosite : PS00769

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