Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
A0006880biological_processintracellular sequestering of iron ion
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
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
B0006880biological_processintracellular sequestering of iron ion
B0006955biological_processimmune response
B0008198molecular_functionferrous iron binding
B0008199molecular_functionferric iron binding
B0008285biological_processnegative regulation of cell population proliferation
B0016020cellular_componentmembrane
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
C0006880biological_processintracellular sequestering of iron ion
C0006955biological_processimmune response
C0008198molecular_functionferrous iron binding
C0008199molecular_functionferric iron binding
C0008285biological_processnegative regulation of cell population proliferation
C0016020cellular_componentmembrane
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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:1992356, ECO:0007744|PDB:1FHA
ChainResidueDetails
AGLU27
AHIS65
BGLU27
BHIS65
CGLU27
CHIS65

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU62
AGLU107
AGLN141
BGLU62
BGLU107
BGLN141
CGLU62
CGLU107
CGLN141

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET0
BMET0
CMET0

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378
ChainResidueDetails
ATHR1
BTHR1
CTHR1

site_idSWS_FT_FI5
Number of Residues3
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
BSER178
CSER178

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008
ChainResidueDetails
ASER182
BSER182
CSER182

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon