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4DYY

Crystal Structure of the Cu-adduct of Human H-Ferritin variant MIC1

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
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 CU A 201
ChainResidue
AGLU27
AGLU62
AHIS65
AHOH315

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 202
ChainResidue
AHIS56
AHIS60
AHIS63
AHIS67
AHOH404

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CU A 203
ChainResidue
AHIS173
AHIS173
AHIS173
AHIS173
AHOH386
AHOH386
AHOH386
AHOH386
AHOH421
AHOH421
AHOH421
AHOH421

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 204
ChainResidue
AASP84
AASP84
AGLN86
AGLN86
AHOH409
AHOH409

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CA A 205
ChainResidue
AASP131
AASP131
AASP131
AGLU134
AGLU134
AGLU134
AHOH446
AHOH446
AHOH446

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
ASER31
ASER59
AHIS60
AHIS63
AHIS63
ATRS207

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 207
ChainResidue
ALEU28
ALEU28
ASER31
ATYR32
ALEU35
ASER59
AHIS63
AILE85
AEDO206
AHOH324
AHOH324

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLADFIEthYLneqvkaIK
ChainResidueDetails
AASP126-LYS146

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

218853

PDB entries from 2024-04-24

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