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6WRV

Crystal structure of computationally designed protein 3DS18 in complex with the human Transferrin receptor ectodomain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004998molecular_functiontransferrin receptor activity
A0033572biological_processtransferrin transport
B0004998molecular_functiontransferrin receptor activity
B0033572biological_processtransferrin transport
E0004998molecular_functiontransferrin receptor activity
E0033572biological_processtransferrin transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues270
DetailsDomain: {"description":"PA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsMotif: {"description":"Cell attachment site; required for binding to transferrin"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000173","evidences":[{"source":"PubMed","id":"10531064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7780197","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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