Structure of PDB 5n26 Chain A Binding Site BS01

Receptor Information
>5n26 Chain A (length=174) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFA
KYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMEC
ALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHV
TNLRKMGAPESGLAEYLFDKHTLG
Ligand information
Ligand IDCPT
InChIInChI=1S/2ClH.2H3N.Pt/h2*1H;2*1H3;/q;;;;+2/p-2
InChIKeyLXZZYRPGZAFOLE-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6[NH3][Pt]([NH3])(Cl)Cl
ACDLabs 12.01[Pt](N)(N)(Cl)Cl
CACTVS 3.385N|[Pt](|N)(Cl)Cl
FormulaCl2 H6 N2 Pt
NameCisplatin;
diammine(dichloro)platinum
ChEMBL
DrugBankDB00515
ZINC
PDB chain5n26 Chain A Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5n26 Cisplatin Binding Sites in Human H-Chain Ferritin.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		K68 H136
Binding residue
(residue number reindexed from 1)		K66 H134
Annotation score1
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:5n26, PDBe:5n26, PDBj:5n26
PDBsum5n26
PubMed28737381
UniProtP02794|FRIH_HUMAN Ferritin heavy chain (Gene Name=FTH1)

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