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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6SOY

Trypanosoma brucei transferrin receptor in complex with human transferrin

Functional Information from GO Data
ChainGOidnamespacecontents
A0042783biological_processsymbiont-mediated evasion of host immune response
B0042783biological_processsymbiont-mediated evasion of host immune response
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005768cellular_componentendosome
C0005769cellular_componentearly endosome
C0005770cellular_componentlate endosome
C0005788cellular_componentendoplasmic reticulum lumen
C0005886cellular_componentplasma membrane
C0005905cellular_componentclathrin-coated pit
C0006811biological_processmonoatomic ion transport
C0006826biological_processiron ion transport
C0006879biological_processintracellular iron ion homeostasis
C0007166biological_processcell surface receptor signaling pathway
C0008198molecular_functionferrous iron binding
C0008199molecular_functionferric iron binding
C0009617biological_processresponse to bacterium
C0009925cellular_componentbasal plasma membrane
C0009986cellular_componentcell surface
C0010008cellular_componentendosome membrane
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0019731biological_processantibacterial humoral response
C0019899molecular_functionenzyme binding
C0030139cellular_componentendocytic vesicle
C0030316biological_processosteoclast differentiation
C0030669cellular_componentclathrin-coated endocytic vesicle membrane
C0031410cellular_componentcytoplasmic vesicle
C0031647biological_processregulation of protein stability
C0031982cellular_componentvesicle
C0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
C0034774cellular_componentsecretory granule lumen
C0034986molecular_functioniron chaperone activity
C0044325molecular_functiontransmembrane transporter binding
C0045178cellular_componentbasal part of cell
C0046872molecular_functionmetal ion binding
C0048260biological_processpositive regulation of receptor-mediated endocytosis
C0048471cellular_componentperinuclear region of cytoplasm
C0055037cellular_componentrecycling endosome
C0060586biological_processmulticellular organismal-level iron ion homeostasis
C0070062cellular_componentextracellular exosome
C0071281biological_processcellular response to iron ion
C0072562cellular_componentblood microparticle
C1990459molecular_functiontransferrin receptor binding
C1990712cellular_componentHFE-transferrin receptor complex
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
ChainResidueDetails
CTYR95-ASP104
CTYR426-SER435
site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
ChainResidueDetails
CTYR188-PHE204
CTYR517-PHE532
site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
ChainResidueDetails
CGLN222-VAL252
CASP558-VAL588
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues322
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000074","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-10-15

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