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1SUV

Structure of Human Transferrin Receptor-Transferrin Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004998molecular_functiontransferrin receptor activity
A0033572biological_processtransferrin transport
B0004998molecular_functiontransferrin receptor activity
B0033572biological_processtransferrin transport
C0005576cellular_componentextracellular region
D0005576cellular_componentextracellular region
E0005576cellular_componentextracellular region
F0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 C 338
ChainResidue
CASP63
CTYR95
CTHR120
CARG124
CALA126
CGLY127
CTYR188
CHIS249
CFE339

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE C 339
ChainResidue
CASP63
CTYR95
CTYR188
CHIS249
CCO3338

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 D 338
ChainResidue
DASP63
DTYR95
DTHR120
DARG124
DALA126
DGLY127
DTYR188
DHIS249
DFE339

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE D 339
ChainResidue
DASP63
DTYR95
DTYR188
DHIS249
DCO3338

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CO3 E 701
ChainResidue
EASP392
ETYR425
ETHR451
EARG455
ETHR456
EALA457
EGLY458
ETYR514
EHIS582
EFE703

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE E 703
ChainResidue
EASP392
ETYR425
ETYR514
EHIS582
ECO3701

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CO3 F 701
ChainResidue
FASP392
FTYR425
FTHR451
FARG455
FTHR456
FALA457
FGLY458
FTYR514
FHIS582
FFE703

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE F 703
ChainResidue
FASP392
FTYR425
FTYR514
FHIS582
FCO3701

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
ChainResidueDetails
CTYR95-ASP104
ETYR425-SER434

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
ChainResidueDetails
CTYR188-PHE204
ETYR514-PHE529

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
ChainResidueDetails
CGLN222-VAL252
EASP555-VAL585

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues180
DetailsDomain: {"description":"PA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues382
DetailsRegion: {"description":"Ligand-binding"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsMotif: {"description":"Cell attachment site; required for binding to transferrin"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
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 Residues2
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 Residues2
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

site_idSWS_FT_FI7
Number of Residues644
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"}
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

246704

PDB entries from 2025-12-24

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