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8E7D

Cryo-EM structure of wild-type transthyretin amyloid from heart tissue

Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV
ChainResidueDetails
ALYS15-VAL30

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS
ChainResidueDetails
ATYR105-SER117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11418763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ICT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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