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2FG4

Structure of Human Ferritin L Chain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005776cellular_componentautophagosome
A0005829cellular_componentcytosol
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
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 191
ChainResidue
AASP131
AASP131
AASP131
AHOH394
AHOH394
AHOH394

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 192
ChainResidue
AASP15
AASP15

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CD A 201
ChainResidue
ACD202
ACD202
ACD204
ACD204
ACD204
AHOH397
AHOH397
AHOH397
ACD202

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CD A 202
ChainResidue
AHIS118
ASER122
ACYS130
AGLU134
ACD201
ACD201
ACD201
AHOH395
AHOH396
AHOH397

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 203
ChainResidue
AHIS136
ACD210

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CD A 204
ChainResidue
ACYS130
AGLU134
AGLU134
ACD201
ACD201
ACD201
AHOH397

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 205
ChainResidue
AGLU60

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 206
ChainResidue
AGLU61
AGLU64
ACD207
AHOH301

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 207
ChainResidue
AGLU61
AGLU140
ACD206
AHOH301

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 208
ChainResidue
AHOH341

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CD A 209
ChainResidue
AGLU90

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 210
ChainResidue
AHIS136
AASP139
ACD203
AHOH384

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 211
ChainResidue
AHIS53
AGLU57

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 Residues149
DetailsDomain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsRegion: {"description":"Catalytic site for iron oxidation"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6653779","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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