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MolNFT v1 · #141891 · protein

Stapled-peptides tailored against initiation of translation

5ZML · Eukaryotic translation initiation factor 4E: “Stapled-peptides tailored against initiation of translation”. X-ray diffraction, 2 ligands (ACE, NO3), 1 pocket (best druggability 0.45). MolNFT v1 #141891 on GenesisL1: 3D structure…

PDB
5ZML
Type
protein
Length
205 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Eukaryotic translation initiation factor 4E; ACE-lys-lys-arg-tyr-ser-arg-MK8-gln-leu-leu-M…
UniProt
P06730
Ligands
ACE, NO3
Pockets
1 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEukaryotic translation initiation factor 4Eprotein19134% helix, 27% strandP06730
BACE-lys-lys-arg-tyr-ser-arg-MK8-gln-leu-leu-MK8-phe-arg- argprotein1443% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains B
  • NO3 · Nitrate ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11470.450.7618EDO

Interfaces

1 interface between chains.

  • A–B · 689 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent (nonstandard, covalent ligand).

Compared structures

  • 5ZML · Stapled-peptides tailored against initiation of translation · the same entry in another collection · chain A against A, TM-score 1.00
  • P06730 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 4E (P06730) · a predicted model of the same protein · chain A against A, TM-score 0.96

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