GL1X · GenesisL1 explorer

MolNFT v1 · #126814 · protein

Crystal structure of EIF4E from C. melo

5ME7 · Eukaryotic transcription initiation factor 4E: “Crystal structure of EIF4E from C. melo”. X-ray diffraction, 5 pockets (best druggability 0.72). MolNFT v1 #126814 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5ME7
Type
protein
Length
703 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Eukaryotic transcription initiation factor 4E
UniProt
Q00LS8
Pockets
5 · best druggability 0.72

Structure

x-ray diffraction · 4 distinct chains · 27% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEukaryotic transcription initiation factor 4Eprotein17529% helix, 31% strandQ00LS8
BEukaryotic transcription initiation factor 4Eprotein17327% helix, 31% strandQ00LS8
CEukaryotic transcription initiation factor 4Eprotein18225% helix, 30% strandQ00LS8
DEukaryotic transcription initiation factor 4Eprotein17327% helix, 31% strandQ00LS8

Ligands and binding sites

  • GOL · Glycerol · additive · 5 copies · chains A, B, C

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110520.720.7696empty
25020.620.7545empty
31760.440.7423empty
41330.390.7429empty
5790.340.7518empty

Interfaces

5 interfaces between chains.

  • B–C · 659 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 361 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 342 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 130 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 97 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5ME7 · Crystal Structure of eiF4E from C. melo · the same entry in another collection · chain A against A, TM-score 1.00

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