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7CK9

Crystal structure of Doxorubicin loaded human ferritin heavy chain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0006955biological_processimmune response
A0008043cellular_componentintracellular ferritin complex
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0008285biological_processnegative regulation of cell population proliferation
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0048147biological_processnegative regulation of fibroblast proliferation
A0070062cellular_componentextracellular exosome
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 Residues4
Detailsbinding site for residue CL A 201
ChainResidue
AHIS173
AHIS173
AHIS173
AHIS173

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 202
ChainResidue
AGLU162
AGLY164
AHOH372
AHOH571

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 203
ChainResidue
AHOH349
AHOH475
AOXY208

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 204
ChainResidue
AGLN14
AHOH487
AHOH562

site_idAC5
Number of Residues8
Detailsbinding site for residue MG A 205
ChainResidue
AHOH330
AHOH330
AHOH332
AHOH332
AHOH540
AHOH540
AHOH588
AHOH588

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 206
ChainResidue
AHOH364
AHOH364
AHOH364
AHOH510
AHOH510
AHOH510

site_idAC7
Number of Residues6
Detailsbinding site for residue MG A 207
ChainResidue
AGLU27
AGLU62
AHIS65
AHOH314
AHOH320
AHOH338

site_idAC8
Number of Residues5
Detailsbinding site for residue OXY A 208
ChainResidue
ALYS157
ASER163
AGLY164
ALEU165
ACL203

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL A 209
ChainResidue
ASER31
AARG63
AARG63

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 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

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PDB entries from 2024-06-12

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