GL1X · GenesisL1 explorer

Research workbench

Structure of the apo EEF2-eta complex

Analyse Structure of the apo EEF2-eta complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZM3
Type
protein
Length
3,090 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor 2; Exotoxin a
EC
2.4.2.36
UniProt
P32324
Pockets
20 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EElongation factor 2protein82337% helix, 26% strandP32324
B, D, FExotoxin a (EC 2.4.2.36)protein20727% helix, 23% strand—

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111150.810.82101empty
29380.790.8170empty
34980.780.8553empty
410530.760.79114empty
510000.760.78102empty

Interfaces

6 interfaces between chains.

  • E–F · 870 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 819 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 814 Ų buried · 2 hydrogen bonds · protein-protein
  • A–F · 309 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 304 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (nonstandard).

Compared structures

  • 1ZM3 · Structure of the apo eEF2-ETA complex · the same entry in another collection · chain F against F, TM-score 1.00
  • P32324 · AlphaFold monomer V2.0 prediction for elongation factor 2 (P32324) · a predicted model of the same protein · chain C against A, TM-score 0.66

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.