Structure of PDB 8pp4 Chain C Binding Site BS02

Receptor Information
>8pp4 Chain C (length=172) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TSQVRQNYHQDSEKAINRQIRLELYASYVYLSMSYYFDRDDVALKNFAKY
FLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDKDDWESGLRAMEKAL
KLEKKVNQSLLELHKLATKKNDPHLCDFIETHYLNEQVKAIKELGDHVTN
LRKMGAPRSGLAEYLFDKHTLG
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 chain8pp4 Chain C Residue 202 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8pp4 Assembly Requirements for the Construction of Large-Scale Binary Protein Structures.
Resolution1.999 Å
Binding residue
(original residue number in PDB)		Y168 L169 K172
Binding residue
(residue number reindexed from 1)		Y164 L165 K168
Annotation score5
Enzymatic activity
Enzyme Commision number 1.16.3.1: ferroxidase.
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:8pp4, PDBe:8pp4, PDBj:8pp4
PDBsum8pp4
PubMed38059469
UniProtP02794|FRIH_HUMAN Ferritin heavy chain (Gene Name=FTH1)

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