Structure of PDB 3s9l Chain C Binding Site BS01

Receptor Information
>3s9l Chain C (length=515) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIA
ANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKK
DSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANF
FSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVA
FVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVA
RSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFL
KVPPRMDAKMYLGYEYVTAIRNLREGTCPPTDECKPVKWCALSHHERLKC
DEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLV
PVLAENYDKSDNCEDTPEAGPNHAVVTRKDKEACVHKILRQQQHLFGSDV
TDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNL
RKCSTSSLLEACTFR
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain3s9l Chain C Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3s9l How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH.
Resolution3.22 Å
Binding residue
(original residue number in PDB)		D63 Y95 Y188 H249
Binding residue
(residue number reindexed from 1)		D60 Y92 Y185 H246
Annotation score4
Enzymatic activity
Enzyme Commision number ?
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

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3s9l, PDBe:3s9l, PDBj:3s9l
PDBsum3s9l
PubMed21788477
UniProtP02787|TRFE_HUMAN Serotransferrin (Gene Name=TF)

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