Structure of PDB 8a2l Chain AAA

Receptor sequence
>8a2lAAA (length=174) Species: 9606 (Homo sapiens) [Search protein sequence]
ASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFA
KYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMEC
ALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHV
TNLRKMGAPESGLAEYLFDKHTLG
3D structure
PDB8a2l A new and efficient procedure to load bioactive molecules within the human heavy-chain ferritin nanocage.
ChainAAA
Resolution2.301 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 FE AAA E27 E62 H65 E25 E60 H63
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:8a2l, PDBe:8a2l, PDBj:8a2l
PDBsum8a2l
PubMed36714262
UniProtP02794|FRIH_HUMAN Ferritin heavy chain (Gene Name=FTH1)

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