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4TQB

The co-complex structure of the translation initiation factor eIF4E with the inhibitor 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003743molecular_functiontranslation initiation factor activity
A0005737cellular_componentcytoplasm
A0006413biological_processtranslational initiation
B0003723molecular_functionRNA binding
B0003743molecular_functiontranslation initiation factor activity
B0005737cellular_componentcytoplasm
B0006413biological_processtranslational initiation
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue MGT A 301
ChainResidue
ATRP56
AHOH523
AHOH531
AHOH533
AHOH536
AHOH544
AHOH574
AHOH605
AHOH624
BTHR55
AMET101
ATRP102
AGLU103
AARG157
ALYS162
AGLY208
AHOH432
AHOH451

site_idAC2
Number of Residues7
Detailsbinding site for residue 34K A 302
ChainResidue
APHE47
ALYS49
AASN59
AARG61
AILE63
AILE79
AHOH406

site_idAC3
Number of Residues8
Detailsbinding site for residue MES A 303
ChainResidue
AVAL69
ALEU135
AARG186
AHOH417
AHOH514
AHOH517
AHOH627
BTRP73

site_idAC4
Number of Residues15
Detailsbinding site for residue MGT B 1000
ChainResidue
AHOH451
BTRP56
BMET101
BTRP102
BGLU103
BARG157
BLYS162
BHOH1117
BHOH1125
BHOH1239
BHOH1243
BHOH1246
BHOH1254
BHOH1268
BHOH1280

Functional Information from PROSITE/UniProt
site_idPS00813
Number of Residues24
DetailsIF4E Eukaryotic initiation factor 4E signature. DYslFKdgIePmWEDeknkrGGRW
ChainResidueDetails
AASP90-TRP113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11879179, ECO:0000269|PubMed:12975586, ECO:0000269|PubMed:16271312
ChainResidueDetails
ATRP56
ATRP102
AARG157
ATHR205
BTRP56
BTRP102
BARG157
BTHR205

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: (Microbial infection) Interaction with potato virus Y VPg => ECO:0000269|PubMed:31712417
ChainResidueDetails
ALYS159
BLYS159

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC and MKNK2 => ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:25923732, ECO:0000269|PubMed:7665584, ECO:0000269|PubMed:7782323
ChainResidueDetails
ASER209
BSER209

237735

PDB entries from 2025-06-18

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