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Complex of D. melanogaster EIF4E with a designed 4E-binding protein (form I)

Analyse Complex of D. melanogaster EIF4E with a designed 4E-binding protein (form I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UEA
Type: protein
Length: 618 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eukaryotic translation initiation factor 4E; Designed 4E-bp
UniProt: P48598
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 5 distinct chains · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eukaryotic translation initiation factor 4E	protein	169	30% helix, 33% strand	P48598
B	Designed 4E-bp	protein	39	56% helix, 3% strand	—
C	Eukaryotic translation initiation factor 4E	protein	167	30% helix, 33% strand	P48598
D, F	Designed 4E-bp	protein	38	39% helix, 3% strand	—
E	Eukaryotic translation initiation factor 4E	protein	167	29% helix, 32% strand	P48598

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	452	0.75	0.84	64	empty
2	101	0.71	0.93	28	empty
3	223	0.65	0.83	25	empty
4	348	0.55	0.75	40	empty
5	111	0.50	0.81	18	empty

Interfaces

7 interfaces between chains.

A–B · 1367 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 1364 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1353 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 728 Å² buried · 6 hydrogen bonds · protein-protein
A–E · 390 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4UEA · Complex of D. melanogaster eIF4E with a designed 4E-binding protein (Form I) · the same entry in another collection · chain F against F, TM-score 1.00
P48598 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E1… · a predicted model of the same protein · chain E against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P48598
Elsewhere: RCSB PDB 4UEA · PDBe 4UEA · UniProt P48598

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