4AZA: Eukaryotic translation initiation factor 4E

Name: PDB 4AZA: Improved eIF4E binding peptides by phage display guided design.
Published: 2012-08-08
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: translation

Improved eIF4E binding peptides by phage display guided design. Determined by X-ray diffraction at 2.16 Å resolution. Released 8 Aug 2012.

Method: X-ray diffraction
Resolution: 2.16 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 3,604
Mol. weight: 54.48 kDa
Ligands: MGO
Released: 8 Aug 2012

Explore 4AZA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AZA contains 27 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: 13 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	31-33	3
β-strand	38-48	11	1
α-helix	57-59	3
β-strand	60-68	9	1
α-helix	69-78	10
α-helix	80-81	2
α-helix	82-84	3
α-helix	86	1
β-strand	90-95	6	1
α-helix	105-108	4
β-strand	111-116	6	1
α-helix	121	1
α-helix	122-126	5
α-helix	127-138	12
α-helix	143-148	6
β-strand	149-155	7	1
β-strand	162-167	6	1
α-helix	173-187	15
β-strand	196-199	4	1
α-helix	200-205	6
β-strand	215-216	2	1

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	56-61	6

Chain C: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	31-33	3
β-strand	38-48	11	2
α-helix	57-59	3
β-strand	60-68	9	2
α-helix	69-76	8
α-helix	80-81	2
α-helix	82-84	3
α-helix	86	1
β-strand	90-95	6	2
β-strand	111-116	6	2
α-helix	121	1
α-helix	122-126	5
α-helix	127-138	12
α-helix	143-148	6
β-strand	149-155	7	2
β-strand	162-167	6	2
α-helix	173-187	15
β-strand	196-199	4	2
α-helix	200-205	6
β-strand	215-216	2	2

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	56-60	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Eukaryotic translation initiation factor 4E	A, C	protein	217	HOMO SAPIENS	P06730 (AlphaFold model)
EIF4G1_D5S peptide	B, D	protein	14	HOMO SAPIENS	Q04637 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4AZA_1 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E (chains A, C)
MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANL
RLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQ
QRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIG
RVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV

Sequence of entity 2 (B, D), FASTA

>4AZA_2 EIF4G1_D5S PEPTIDE (chains B, D)
XKKRYSREFLLGFX

Ligands and cofactors

ID	Name	Formula	Copies
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 P3	2

Primary citation

Improved Eif4E Binding Peptides by Phage Display Guided Design: Plasticity of Interacting Surfaces Yield Collective Effects. Zhou, W., Quah, S.T., Verma, C.S. et al. PLoS One (2012) 7:47235. DOI 10.1371/JOURNAL.PONE.0047235 · PubMed

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

4TPW 1.5 Å, The co-complex structure of the translation initiation factor eIF4E with the inhibitor…
5T46 1.53 Å, Crystal structure of the human eIF4E-eIF4G complex
8QM8 1.58 Å, Potential drug binding sites for translation initiation factor eIF4E
4TQB 1.59 Å, The co-complex structure of the translation initiation factor eIF4E with the inhibitor…
5ZJY 1.59 Å, Stapled-peptides tailored against initiation of translation
7D6Y 1.67 Å, eIF4E in Complex with a Disulphide-Free Autonomous VH Domain
5ZJZ 1.67 Å, Stapled-peptides tailored against initiation of translation
5EI3 1.71 Å, Co-crystal structure of eIF4E with nucleotide mimetic inhibitor.
4UED 1.75 Å, Complex of human eIF4E with the 4E binding protein 4E-BP1
5ZK9 1.76 Å, Stapled-peptides tailored against initiation of translation
4TQC 1.8 Å, The co-complex structure of the translation initiation factor eIF4E with the inhibitor…
5ZML 1.8 Å, Stapled-peptides tailored against initiation of translation

Browse structure collections

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