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6SHT

Molecular structure of mouse apoferritin resolved at 2.7 Angstroms with the Glacios cryo-microscope

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
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
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
A0140315molecular_functioniron ion sequestering activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue FE A 201
ChainResidue
AHIS170

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 202
ChainResidue
AGLU24
AHIS62
AGLU137
AHOH308

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEtyYLseqvksIK
ChainResidueDetails
AASP123-LYS143

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR
ChainResidueDetails
AGLU58-ARG76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU24
AGLU59
AHIS62
AGLU104
AGLN138

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P02794
ChainResidueDetails
AMET-3

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0000250|UniProtKB:P02794
ChainResidueDetails
ATHR-2

224201

PDB entries from 2024-08-28

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