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3F34

Apoferritin: complex with 2,6-diethylphenol

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
A0006880biological_processintracellular sequestering of iron ion
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 Residues5
DetailsBINDING SITE FOR RESIDUE CD A 1001
ChainResidue
AASP80
AASP80
AGLN82
AGLN82
AHOH309

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CD A 1002
ChainResidue
AHOH186
AHOH186
AHOH187
AGLU130
AGLU130
AGLU130
AHOH186

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 1003
ChainResidue
AGLU56
AGLU57
AGLU60

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 1004
ChainResidue
AGLU53
AGLU56

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 1005
ChainResidue
AASP127
AASP127
AASP127

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DIE A 2001
ChainResidue
ALEU24
ASER27
ATYR28
AARG59
ALEU81

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 3001
ChainResidue
AGLN6
AASN7
AHOH182
AHOH243
AHOH254
AHOH262

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 3002
ChainResidue
AGLU45
ALYS143
AASP146
AHOH219
AHOH268
AHOH283
AHOH303
AHOH357

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 3003
ChainResidue
AARG25
ASER85

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 3004
ChainResidue
AASP127
ASER131
AHIS132
AASP135
AHOH229

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 2024-08-28

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