Structure of PDB 4h0w Chain A

Receptor sequence
>4h0wA (length=679) Species: 9606 (Homo sapiens) [Search protein sequence]
VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIR
AIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAV
VKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAV
ANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAG
DVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHT
VVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAH
GFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHH
ERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAG
KCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSC
HTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMG
SGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPW
AKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKI
LRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKY
LGEEYVKAVGNLRKCSTSSLLEACTFRRP
3D structure
PDB4h0w Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe.
ChainA
Resolution2.4 Å
3D
structure
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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 D392 Y426 Y517 H585
BS02 CO3 A D392 T452 R456 T457 A458 G459 Y517 D392 T452 R456 T457 A458 G459 Y517
BS03 CO3 A T120 R124 S125 A126 G127 Y188 T120 R124 S125 A126 G127 Y188
BS04 NTA A D63 Y95 S125 K296 D63 Y95 S125 K296
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
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Cellular Component
External links
PDB RCSB:4h0w, PDBe:4h0w, PDBj:4h0w
PDBsum4h0w
PubMed23256035
UniProtP02787|TRFE_HUMAN Serotransferrin (Gene Name=TF)

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