GL1X · GenesisL1 explorer

MolNFT v1 · #150948 · protein

Beta-phosphoglucomutase from lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.8 a.

6H8X: “Beta-phosphoglucomutase from lactococcus lactis in an open conformer complexed with magnesium trifluoride to…”. X-ray diffraction, 2 ligands (MGF, MG), 2 pockets (best druggability 0.74). MolNFT v1 #150948 on GenesisL1: 3D…

PDB
6H8X
Type
protein
Length
438 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-phosphoglucomutase
EC
5.4.2.6
UniProt
P71447
Ligands
MGF, MG
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta-phosphoglucomutase (EC 5.4.2.6)protein21953% helix, 11% strandP71447

Ligands and binding sites

  • MGF · Trifluoromagnesate · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
  • ACT · Acetate ion · additive · chains A
  • PDO · 1,3-propandiol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16790.740.8057EDO, MGF
27300.710.7856EDO, MGF, ACT

Interfaces

1 interface between chains.

  • A–B · 598 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6H8X · Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P71447 · AlphaFold monomer V2.0 prediction for beta-phosphoglucomutase (P71447) · a predicted model of the same protein · chain A against A, TM-score 0.86

Analyse

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