GL1X · GenesisL1 explorer

Research workbench

Crystal structure of methanoperedens nitroreducens elongation factor 2 H595N bound to gmppcp and magnesium (triclinic crystal form)

Analyse Crystal structure of methanoperedens nitroreducens elongation factor 2 H595N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6U43
Type
protein
Length
723 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor 2
UniProt
A0A062V290
Ligands
GCP, MG, SO4, CL
Pockets
7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElongation factor 2protein72339% helix, 27% strandA0A062V290

Ligands and binding sites

  • GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • CL · Chloride ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111380.760.79113empty
25190.730.8247empty
35690.700.7966empty
41060.540.8320empty
51030.440.7924GCP, MG

Compared structures

  • 6U43 · Crystal structure of Methanoperedens nitroreducens elongation factor 2 H595N bound to… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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