2W97: EIF4E

Crystal Structure of eIF4E Bound to Glycerol and eIF4G1 peptide. Determined by X-ray diffraction at 2.29 Å resolution. Released 31 Mar 2010.

Method
X-ray diffraction
Resolution
2.29 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
3,483
Mol. weight
55.23 kDa
Ligands
MGO
Released
31 Mar 2010

Explore 2W97 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2W97 contains 23 α-helices and 16 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand38-48111
α-helix57-593
β-strand60-6891
α-helix69-7810
α-helix82-843
α-helix861
β-strand90-9561
β-strand111-11661
α-helix119-1213
α-helix122-1265
α-helix127-13812
α-helix143-1486
β-strand149-15571
β-strand162-16761
α-helix173-18715
β-strand196-19941
α-helix200-2045
α-helix212-2132
β-strand215-21621
Chain B: 10 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix31-333
β-strand38-49122
β-strand60-6892
α-helix69-7810
α-helix82-843
α-helix861
β-strand89-9572
β-strand111-11662
α-helix119-1213
α-helix122-1265
α-helix127-13812
α-helix143-1486
β-strand149-15572
β-strand162-16762
α-helix173-18614
β-strand196-19942
α-helix200-2056
β-strand215-21622
Chain E: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix626-6316
Chain F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix626-6305

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Eukaryotic translation initiation factor 4EAprotein217HOMO SAPIENSP06730 (AlphaFold model)
Eukaryotic translation initiation factor 4EBprotein217HOMO SAPIENSP06730 (AlphaFold model)
Eukaryotic translation initiation factor 4 gamma 1E, Fprotein14HOMO SAPIENSQ04637 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2W97_1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E (chains A)
MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANL
RLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQ
QRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIG
RVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
Sequence of entity 2 (B), FASTA
>2W97_2 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E (chains B)
MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKKDKSKTWQANL
RLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQ
QRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIG
RVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
Sequence of entity 3 (E, F), FASTA
>2W97_3 EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1 (chains E, F)
KKRYDREFLLGFQF

Ligands and cofactors

IDNameFormulaCopies
MGO[[(2R,3S,4R,5R)-5-(6-amino-3-methyl-4-oxo-5H-IMIDAZO[4,5-c]pyridin-1-yl)-3,4-di…C12 H20 N4 O14 P31

Water and common crystallization additives (GOL, SO4, PGE) are not listed.

Primary citation

Crystallization of eIF4E complexed with eIF4GI peptide and glycerol reveals distinct structural differences around the cap-binding site. Brown, C.J., Verma, C.S., Walkinshaw, M.D. et al. Cell Cycle (2009) 8:1905-1911. DOI 10.4161/cc.8.12.8742 · PubMed

Other PDB entries of the same protein (UniProt P06730 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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