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7A4M

Cryo-EM structure of mouse heavy-chain apoferritin at 1.22 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005776cellular_componentautophagosome
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006955biological_processimmune response
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0008285biological_processnegative regulation of cell population proliferation
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0031410cellular_componentcytoplasmic vesicle
A0042802molecular_functionidentical protein binding
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0048147biological_processnegative regulation of fibroblast proliferation
A0071682cellular_componentendocytic vesicle lumen
A0110076biological_processnegative regulation of ferroptosis
Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEtyYLseqvksIK
ChainResidueDetails
AASP126-LYS146

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR
ChainResidueDetails
AGLU61-ARG79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues149
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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