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6WYH

Crystal structure of Human H-chain Ferritin variant 157C Delta C-star Modified with a RAFT Agent Soaked in an Acrylate Solution

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_componentobsolete intracellular 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
B0004322molecular_functionferroxidase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0006880biological_processintracellular sequestering of iron ion
B0006955biological_processimmune response
B0008043cellular_componentobsolete intracellular ferritin complex
B0008198molecular_functionferrous iron binding
B0008199molecular_functionferric iron binding
B0008285biological_processnegative regulation of cell population proliferation
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0044754cellular_componentautolysosome
B0046872molecular_functionmetal ion binding
B0048147biological_processnegative regulation of fibroblast proliferation
B0070062cellular_componentextracellular exosome
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
C0005829cellular_componentcytosol
C0006826biological_processiron ion transport
C0006879biological_processintracellular iron ion homeostasis
C0006880biological_processintracellular sequestering of iron ion
C0006955biological_processimmune response
C0008043cellular_componentobsolete intracellular ferritin complex
C0008198molecular_functionferrous iron binding
C0008199molecular_functionferric iron binding
C0008285biological_processnegative regulation of cell population proliferation
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0042802molecular_functionidentical protein binding
C0044754cellular_componentautolysosome
C0046872molecular_functionmetal ion binding
C0048147biological_processnegative regulation of fibroblast proliferation
C0070062cellular_componentextracellular exosome
C0110076biological_processnegative regulation of ferroptosis
C0140315molecular_functioniron ion sequestering activity
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
D0004322molecular_functionferroxidase activity
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006826biological_processiron ion transport
D0006879biological_processintracellular iron ion homeostasis
D0006880biological_processintracellular sequestering of iron ion
D0006955biological_processimmune response
D0008043cellular_componentobsolete intracellular ferritin complex
D0008198molecular_functionferrous iron binding
D0008199molecular_functionferric iron binding
D0008285biological_processnegative regulation of cell population proliferation
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0042802molecular_functionidentical protein binding
D0044754cellular_componentautolysosome
D0046872molecular_functionmetal ion binding
D0048147biological_processnegative regulation of fibroblast proliferation
D0070062cellular_componentextracellular exosome
D0110076biological_processnegative regulation of ferroptosis
D0140315molecular_functioniron ion sequestering activity
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue FE A 201
ChainResidue
AGLU27
AGLU62
AHIS65
AFE202

site_idAC2
Number of Residues5
Detailsbinding site for residue FE A 202
ChainResidue
AGLU62
AGLU107
AGLN141
AFE201
AFE204

site_idAC3
Number of Residues4
Detailsbinding site for residue FE A 203
ChainResidue
AHIS173
BHIS173
CHIS173
DHIS173

site_idAC4
Number of Residues4
Detailsbinding site for residue FE A 204
ChainResidue
AGLU62
AGLU107
AFE202
AHOH460

site_idAC5
Number of Residues4
Detailsbinding site for residue RFT A 205
ChainResidue
ACYS157
AHOH302
BGLY164
BHOH303

site_idAC6
Number of Residues7
Detailsbinding site for residue FE B 201
ChainResidue
BGLU27
BGLU62
BHIS65
BGLN141
BFE202
BHOH371
BHOH387

site_idAC7
Number of Residues7
Detailsbinding site for residue FE B 202
ChainResidue
BGLU62
BGLU107
BGLN141
BFE201
BHOH324
BHOH371
BHOH387

site_idAC8
Number of Residues4
Detailsbinding site for residue CA B 203
ChainResidue
AASP84
AGLN86
BASP84
BGLN86

site_idAC9
Number of Residues6
Detailsbinding site for residue CA B 204
ChainResidue
AHOH312
AHOH348
AHOH362
AHOH424
BHOH323
BHOH460

site_idAD1
Number of Residues5
Detailsbinding site for residue CA B 205
ChainResidue
AHOH312
AHOH393
AHOH422
BHOH323
BHOH486

site_idAD2
Number of Residues4
Detailsbinding site for residue FE C 201
ChainResidue
CGLU27
CGLU62
CHIS65
CHOH307

site_idAD3
Number of Residues5
Detailsbinding site for residue FE C 202
ChainResidue
CGLU62
CGLU107
CGLN141
CHOH307
CHOH347

site_idAD4
Number of Residues7
Detailsbinding site for residue CA C 203
ChainResidue
AASP131
AGLU134
BASP131
BGLU134
CASP131
CGLU134
CCA204

site_idAD5
Number of Residues6
Detailsbinding site for residue CA C 204
ChainResidue
AGLU134
AHOH325
BGLU134
CGLU134
CCA203
CHOH301

site_idAD6
Number of Residues4
Detailsbinding site for residue FE D 201
ChainResidue
DGLU27
DGLU62
DHIS65
DFE202

site_idAD7
Number of Residues4
Detailsbinding site for residue FE D 202
ChainResidue
DGLU62
DGLU107
DGLN141
DFE201

site_idAD8
Number of Residues12
Detailsbinding site for residue CA D 203
ChainResidue
DASP131
DASP131
DASP131
DGLU134
DGLU134
DGLU134
DCA204
DCA204
DCA204
DHOH322
DHOH322
DHOH322

site_idAD9
Number of Residues9
Detailsbinding site for residue CA D 204
ChainResidue
DHOH311
DHOH311
DGLU134
DGLU134
DGLU134
DCA203
DCA203
DCA203
DHOH311

site_idAE1
Number of Residues10
Detailsbinding site for residue RFT B 206
ChainResidue
BTHR153
BASN154
BLEU155
BARG156
BMET158
BGLY159
BHOH305
BHOH328
BHOH412
DGLY164

site_idAE2
Number of Residues7
Detailsbinding site for residue RFT C 205
ChainResidue
AGLY164
CTHR153
CASN154
CLEU155
CARG156
CMET158
CGLY159

site_idAE3
Number of Residues7
Detailsbinding site for Di-peptide RFT D 205 and CYS D 157
ChainResidue
CGLY164
DTHR153
DASN154
DLEU155
DARG156
DMET158
DGLY159

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLADFIEthYLneqvkaIK
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 Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:1992356, ECO:0007744|PDB:1FHA
ChainResidueDetails
AGLU27
AHIS65
BGLU27
BHIS65
CGLU27
CHIS65
DGLU27
DHIS65

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU62
DGLU62
DGLU107
DGLN141
AGLU107
AGLN141
BGLU62
BGLU107
BGLN141
CGLU62
CGLU107
CGLN141

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378
ChainResidueDetails
ATHR1
BTHR1
CTHR1
DTHR1

site_idSWS_FT_FI4
Number of Residues4
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
DSER178

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008
ChainResidueDetails
ASER182
BSER182
CSER182
DSER182

222036

PDB entries from 2024-07-03

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