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5LG8

Human L-type ferritin iron loaded for 60 minutes

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005776cellular_componentautophagosome
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006880biological_processintracellular sequestering of iron ion
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0016020cellular_componentmembrane
A0031410cellular_componentcytoplasmic vesicle
A0035578cellular_componentazurophil granule lumen
A0042802molecular_functionidentical protein binding
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0055072biological_processobsolete iron ion homeostasis
A0070062cellular_componentextracellular exosome
A0070288cellular_componentferritin complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CD A 201
ChainResidue
AASP15
AASP15
AHOH432
AHOH432
AHOH445
AHOH445

site_idAC2
Number of Residues3
Detailsbinding site for residue CD A 202
ChainResidue
AASP131
AASP131
AASP131

site_idAC3
Number of Residues3
Detailsbinding site for residue CD A 203
ChainResidue
ACYS130
AGLU134
AGLU134

site_idAC4
Number of Residues4
Detailsbinding site for residue CD A 204
ChainResidue
AHIS118
ACYS130
AGLU134
AHOH484

site_idAC5
Number of Residues3
Detailsbinding site for residue CD A 205
ChainResidue
AHIS136
AHOH449
AHOH464

site_idAC6
Number of Residues4
Detailsbinding site for residue CD A 206
ChainResidue
AGLU90
AHOH395
AHOH416
AHOH450

site_idAC7
Number of Residues2
Detailsbinding site for residue CD A 207
ChainResidue
AGLU49
AASP178

site_idAC8
Number of Residues1
Detailsbinding site for residue CD A 208
ChainResidue
AGLU90

site_idAC9
Number of Residues8
Detailsbinding site for residue FE A 209
ChainResidue
AGLU61
AGLU64
AFE210
AFE211
AOXY213
APER214
APER216
AHOH383

site_idAD1
Number of Residues8
Detailsbinding site for residue FE A 210
ChainResidue
AGLU57
AGLU60
AGLU61
AFE209
AFE211
AOXY213
APER215
APER216

site_idAD2
Number of Residues8
Detailsbinding site for residue FE A 211
ChainResidue
AGLU60
AGLU64
AFE209
AFE210
AOXY213
APER214
APER215
AHOH382

site_idAD3
Number of Residues4
Detailsbinding site for residue FE A 212
ChainResidue
AGLU57
APER215
AHOH457
AHOH496

site_idAD4
Number of Residues9
Detailsbinding site for residue OXY A 213
ChainResidue
AGLU60
AGLU61
AGLU64
AFE209
AFE210
AFE211
APER214
APER215
APER216

site_idAD5
Number of Residues6
Detailsbinding site for residue PER A 214
ChainResidue
AGLU64
AFE209
AFE211
AOXY213
APER216
AHOH383

site_idAD6
Number of Residues7
Detailsbinding site for residue PER A 215
ChainResidue
AGLU57
AGLU60
AFE210
AFE211
AFE212
AOXY213
AHOH388

site_idAD7
Number of Residues6
Detailsbinding site for residue PER A 216
ChainResidue
AGLU57
AGLU61
AFE209
AFE210
AOXY213
APER214

site_idAD8
Number of Residues9
Detailsbinding site for residue SO4 A 217
ChainResidue
ASER13
AASP15
AARG124
AARG124
AHOH318
AHOH327
AHOH364
AHOH415
AHOH432

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

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EkREgyERLLkmQNqRgGR
ChainResidueDetails
AGLU61-ARG79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLU57
AGLU60
AGLU61
AGLU64
AGLU67

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6653779
ChainResidueDetails
ASER5

223166

PDB entries from 2024-07-31

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