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MolNFT v1 · #144130 · protein

1.83 ångström resolution crystal structure of N-terminal fragment (residues 1-404) of elongation factor G from enterococcus faecalis

6BK7: “1.83 ångström resolution crystal structure of N-terminal fragment (residues 1-404) of elongation factor G…”. X-ray diffraction, 1 ligand (NA), 12 pockets (best druggability 0.71). MolNFT v1 #144130 on GenesisL1: 3D structure…

PDB
6BK7
Type
protein
Length
760 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor G
UniProt
Q839G9
Ligands
NA
Pockets
12 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BElongation factor Gprotein38027% helix, 32% strandQ839G9

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1700.710.9623empty
2740.710.9627empty
32080.640.8428NA
41840.630.8428NA
5980.500.8224empty

Compared structures

  • 6BK7 · 1.83 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-404) of… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q839G9 · AlphaFold monomer V2.0 prediction for elongation factor G (Q839G9) · a predicted model of the same protein · chain B against A, TM-score 0.96

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