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8J9M

Crystal Structure of Human H-Ferritin variant 123F assembling in solution3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
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
A0016491molecular_functionoxidoreductase activity
A0031410cellular_componentcytoplasmic vesicle
A0042802molecular_functionidentical protein binding
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0048147biological_processnegative regulation of fibroblast proliferation
A0070062cellular_componentextracellular exosome
A0070288cellular_componentferritin complex
A0110076biological_processnegative regulation of ferroptosis
A0140315molecular_functioniron ion sequestering activity
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0004322molecular_functionferroxidase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005776cellular_componentautophagosome
B0005829cellular_componentcytosol
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0006955biological_processimmune response
B0008198molecular_functionferrous iron binding
B0008199molecular_functionferric iron binding
B0008285biological_processnegative regulation of cell population proliferation
B0016491molecular_functionoxidoreductase activity
B0031410cellular_componentcytoplasmic vesicle
B0042802molecular_functionidentical protein binding
B0044754cellular_componentautolysosome
B0046872molecular_functionmetal ion binding
B0048147biological_processnegative regulation of fibroblast proliferation
B0070062cellular_componentextracellular exosome
B0070288cellular_componentferritin complex
B0110076biological_processnegative regulation of ferroptosis
B0140315molecular_functioniron ion sequestering activity
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
C0004322molecular_functionferroxidase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005764cellular_componentlysosome
C0005776cellular_componentautophagosome
C0005829cellular_componentcytosol
C0006826biological_processiron ion transport
C0006879biological_processintracellular iron ion homeostasis
C0006955biological_processimmune response
C0008198molecular_functionferrous iron binding
C0008199molecular_functionferric iron binding
C0008285biological_processnegative regulation of cell population proliferation
C0016491molecular_functionoxidoreductase activity
C0031410cellular_componentcytoplasmic vesicle
C0042802molecular_functionidentical protein binding
C0044754cellular_componentautolysosome
C0046872molecular_functionmetal ion binding
C0048147biological_processnegative regulation of fibroblast proliferation
C0070062cellular_componentextracellular exosome
C0070288cellular_componentferritin complex
C0110076biological_processnegative regulation of ferroptosis
C0140315molecular_functioniron ion sequestering activity
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLneqvkaIK
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 Residues447
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1992356","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FHA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Essential for association with cargo receptor NCOA4","evidences":[{"source":"PubMed","id":"26436293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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