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3AJQ

Crystal structure of human H ferritin E140Q mutant

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 183
ChainResidue
AGLU27
AGLU62
AHIS65
AHOH228
AHOH269
AHOH270

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 184
ChainResidue
AHOH272
AHOH273
AHOH381
AGLN58
AGLU61
AHOH271

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 185
ChainResidue
AHOH292
AHOH292
AHOH293
AHOH293
AHOH295
AHOH295
AHOH296
AHOH296

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 186
ChainResidue
AHOH246
AHOH246
AHOH246
AHOH253
AHOH253
AHOH253

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 187
ChainResidue
AHOH311
AHOH312
AHOH313
AHOH314
AHOH315
AHOH316

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 188
ChainResidue
AASP131
AGLU134
AHOH363
AHOH363

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 189
ChainResidue
AHIS173
AHIS173
AHIS173
AHIS173

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 190
ChainResidue
AHIS173
AHIS173
AHIS173

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 191
ChainResidue
AASN25
AGLN83
AHOH224

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 192
ChainResidue
AHOH331
AHOH337

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 193
ChainResidue
ALYS49
AASP150
AHOH199
AHOH209
AHOH318

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLnqqvkaIK
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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:1992356, ECO:0007744|PDB:1FHA
ChainResidueDetails
AGLU27
AHIS65

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU62
AGLU107
AGLN141

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Essential for association with cargo receptor NCOA4 => ECO:0000269|PubMed:26436293
ChainResidueDetails
AARG22

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378
ChainResidueDetails
ATHR1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER178

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008
ChainResidueDetails
ASER182

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PDB entries from 2025-06-18

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