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6JEE

Crystal structure of apo-L161C/L165C-Fr

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005776cellular_componentautophagosome
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0031410cellular_componentcytoplasmic vesicle
A0044754cellular_componentautolysosome
A0046872molecular_functionmetal ion binding
A0070288cellular_componentferritin complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue CD A 201
ChainResidue
AGLU130
AGLU130
AGLU130
AHOH334
AHOH334
AHOH334
AHOH352
AHOH352
AHOH352

site_idAC2
Number of Residues6
Detailsbinding site for residue CD A 202
ChainResidue
AHOH305
AHOH305
AHOH305
AHOH307
AHOH307
AHOH307

site_idAC3
Number of Residues4
Detailsbinding site for residue CD A 203
ChainResidue
AASP80
AASP80
ACL210
ACL210

site_idAC4
Number of Residues5
Detailsbinding site for residue CD A 204
ChainResidue
ACYS161
ACYS165
ACD205
ACD205
AHOH478

site_idAC5
Number of Residues8
Detailsbinding site for residue CD A 205
ChainResidue
ACYS165
ACYS165
ACD204
ACD204
AHOH508
AHOH508
AHOH508
AHOH508

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 A 206
ChainResidue
AGLN6
AASN7
AHOH304
AHOH320
AHOH377
AHOH437

site_idAC7
Number of Residues8
Detailsbinding site for residue SO4 A 207
ChainResidue
AGLU45
ALYS143
AASP146
AHOH313
AHOH328
AHOH374
AHOH398
AHOH420

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 208
ChainResidue
AGLU11
AARG18
AHOH365
AHOH368
AHOH415

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 209
ChainResidue
ALYS104
AHOH302
AHOH314
AHOH452

site_idAD1
Number of Residues5
Detailsbinding site for residue CL A 210
ChainResidue
AASP80
AGLN82
ALYS83
ACD203
ACD203

Functional Information from PROSITE/UniProt
site_idPS00204
Number of Residues21
DetailsFERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFLEshFLdeevklIK
ChainResidueDetails
AASP122-LYS142

site_idPS00540
Number of Residues19
DetailsFERRITIN_1 Ferritin iron-binding regions signature 1. EkREgaERLLkmQNqRgGR
ChainResidueDetails
AGLU57-ARG75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085
ChainResidueDetails
AGLU53
AGLU56
AGLU57
AGLU60
AGLU63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7026284
ChainResidueDetails
ASER1

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PDB entries from 2025-06-11

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