Structure of PDB 3s9n Chain C Binding Site BS02

Receptor Information
>3s9n Chain C (length=511) 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
KVPPRMDAKMYLGYEYVTAIRNLREGTCECKPVKWCALSHHERLKCDEWS
VNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLA
ENYDKSDNCEDTPEAGPNHAVVTRKDKEACVHKILRQQQHLFGSDVTDCS
GNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCS
TSSLLEACTFR
Ligand information
Ligand IDCO3
InChIInChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-2
InChIKeyBVKZGUZCCUSVTD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(=O)([O-])[O-]
ACDLabs 10.04
CACTVS 3.341		[O-]C([O-])=O
FormulaC O3
NameCARBONATE ION
ChEMBL
DrugBankDB14531
ZINC
PDB chain3s9n Chain C Residue 905 [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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PDB3s9n How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH.
Resolution3.25 Å
Binding residue
(original residue number in PDB)		D63 T120 R124 S125 A126 Y188
Binding residue
(residue number reindexed from 1)		D60 T117 R121 S122 A123 Y185
Annotation score3
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3s9n, PDBe:3s9n, PDBj:3s9n
PDBsum3s9n
PubMed21788477
UniProtP02787|TRFE_HUMAN Serotransferrin (Gene Name=TF)

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