6OKD

Crystal Structure of human transferrin receptor in complex with a cystine-dense peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004998	molecular_function	transferrin receptor activity
A	0033572	biological_process	transferrin transport
B	0004998	molecular_function	transferrin receptor activity
B	0033572	biological_process	transferrin transport

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	180
Details	Domain: {"description":"PA"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Motif: {"description":"Cell attachment site; required for binding to transferrin"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

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