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3ES3

Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. The Complex with Gold ions. Ferritin H8-H9x 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
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AU A 731
ChainResidue
AHIS57
AHIS60
AHOH737
AHOH786

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE AU A 732
ChainResidue
AHIS65
AHIS136
ACYS140

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AU A 733
ChainResidue
APRO127
AHOH770
AHIS118
ALYS119

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE AU A 734
ChainResidue
AHIS173

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 735
ChainResidue
AASP131
AGLU134

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 736
ChainResidue
AASP84
AGLN86

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLSDFIEthYLncqvcaIK
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

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET0

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 2024-07-24

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