Structure of PDB 5wtd Chain A

Receptor sequence
>5wtdA (length=649) Species: 9606 (Homo sapiens) [Search protein sequence]
DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAI
AANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVK
KDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVAN
FFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV
AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVV
ARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGF
LKVPPRMDAKMYLGYEYVTAIRNLREGTCPCKPVKWCALSHHERLKCDEW
SVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVL
AENYNAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLY
NKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYT
GAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTR
KPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNSETKDLL
FRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
3D structure
PDB5wtd Binding of ruthenium and osmium at non‐iron sites of transferrin accounts for their iron-independent cellular uptake.
ChainA
Resolution2.501 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE A D392 Y426 Y517 H585 D384 Y408 Y499 H567
BS02 RU A H14 H289 H12 H287
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008198 ferrous iron binding
GO:0008199 ferric iron binding
GO:0019899 enzyme binding
GO:0034986 iron chaperone activity
GO:0044325 transmembrane transporter binding
GO:0046872 metal ion binding
GO:1990459 transferrin receptor binding
Biological Process
GO:0006826 iron ion transport
GO:0006879 intracellular iron ion homeostasis
GO:0007015 actin filament organization
GO:0009617 response to bacterium
GO:0019731 antibacterial humoral response
GO:0030316 osteoclast differentiation
GO:0031647 regulation of protein stability
GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0034756 regulation of iron ion transport
GO:0042327 positive regulation of phosphorylation
GO:0045780 positive regulation of bone resorption
GO:0045893 positive regulation of DNA-templated transcription
GO:0048260 positive regulation of receptor-mediated endocytosis
GO:0060586 multicellular organismal-level iron ion homeostasis
GO:0070371 ERK1 and ERK2 cascade
GO:0071281 cellular response to iron ion
GO:2000147 positive regulation of cell motility
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005768 endosome
GO:0005769 early endosome
GO:0005770 late endosome
GO:0005788 endoplasmic reticulum lumen
GO:0005886 plasma membrane
GO:0005905 clathrin-coated pit
GO:0009925 basal plasma membrane
GO:0009986 cell surface
GO:0010008 endosome membrane
GO:0016020 membrane
GO:0016324 apical plasma membrane
GO:0030139 endocytic vesicle
GO:0030669 clathrin-coated endocytic vesicle membrane
GO:0031410 cytoplasmic vesicle
GO:0031982 vesicle
GO:0034774 secretory granule lumen
GO:0045178 basal part of cell
GO:0048471 perinuclear region of cytoplasm
GO:0055037 recycling endosome
GO:0070062 extracellular exosome
GO:0072562 blood microparticle
GO:1990712 HFE-transferrin receptor complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5wtd, PDBe:5wtd, PDBj:5wtd
PDBsum5wtd
PubMed35690040
UniProtP02787|TRFE_HUMAN Serotransferrin (Gene Name=TF)

[Back to BioLiP]