Structure of PDB 3es3 Chain A

Receptor sequence
>3es3A (length=172) Species: 9606 (Homo sapiens) [Search protein sequence]
TSQVRQNYDQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKY
FLHQSHEERCHAEKLMKLQNQRGGRIFLQDIQKPDRDDWESGLNAMEAAL
QLEKNVNQSLLELHKLATDKNDPHLSDFIETHYLNCQVCAIKCLGDHVTN
LRKMGAPESGLAEYLFDKHTLG
3D structure
PDB3es3 Directing noble metal ion chemistry within a designed ferritin protein.
ChainA
Resolution2.795 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.16.3.1: ferroxidase.
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 AU A H57 H60 H53 H56
BS02 AU A H65 C140 H61 C136
BS03 CA A D131 E134 D127 E130
Gene Ontology
Molecular Function
GO:0004322 ferroxidase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008198 ferrous iron binding
GO:0008199 ferric iron binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0140315 iron ion sequestering activity
Biological Process
GO:0006826 iron ion transport
GO:0006879 intracellular iron ion homeostasis
GO:0006880 intracellular sequestering of iron ion
GO:0006955 immune response
GO:0008285 negative regulation of cell population proliferation
GO:0048147 negative regulation of fibroblast proliferation
GO:0110076 negative regulation of ferroptosis
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005776 autophagosome
GO:0005829 cytosol
GO:0016020 membrane
GO:0031410 cytoplasmic vesicle
GO:0044754 autolysosome
GO:0070062 extracellular exosome
GO:0070288 ferritin complex
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3es3, PDBe:3es3, PDBj:3es3
PDBsum3es3
PubMed18991401
UniProtP02794|FRIH_HUMAN Ferritin heavy chain (Gene Name=FTH1)

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