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1CX8

CRYSTAL STRUCTURE OF THE ECTODOMAIN OF HUMAN TRANSFERRIN RECEPTOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004998molecular_functiontransferrin receptor activity
A0033572biological_processtransferrin transport
B0004998molecular_functiontransferrin receptor activity
B0033572biological_processtransferrin transport
C0004998molecular_functiontransferrin receptor activity
C0033572biological_processtransferrin transport
D0004998molecular_functiontransferrin receptor activity
D0033572biological_processtransferrin transport
E0004998molecular_functiontransferrin receptor activity
E0033572biological_processtransferrin transport
F0004998molecular_functiontransferrin receptor activity
F0033572biological_processtransferrin transport
G0004998molecular_functiontransferrin receptor activity
G0033572biological_processtransferrin transport
H0004998molecular_functiontransferrin receptor activity
H0033572biological_processtransferrin transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues720
DetailsDomain: {"description":"PA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1528
DetailsRegion: {"description":"Ligand-binding"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsMotif: {"description":"Cell attachment site; required for binding to transferrin"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
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_FI5
Number of Residues8
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_FI6
Number of Residues8
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

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
AGLY456

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
BGLY456

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
CGLY456

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
DGLY456

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
EGLY456

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
FGLY456

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
GGLY456

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1amp
ChainResidueDetails
HGLY456

245011

PDB entries from 2025-11-19

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