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Beta-phosphoglucomutase from lactococcus lactis with citrate, tris and acetate bound

Analyse Beta-phosphoglucomutase from lactococcus lactis with citrate, tris and acetate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YDM
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
MG
Pockets
3 · best druggability 0.71

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

  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • ACT · Acetate ion · additive · 2 copies · chains A, B
  • CIT · Citric acid · additive · chains A
  • PDO · 1,3-propandiol · additive · chains A
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B
  • EDO · 1,2-ethanediol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14300.710.8239CIT, ACT
24640.690.8050ACT, TRS
31050.410.7723empty

Interfaces

1 interface between chains.

  • A–B · 577 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 6YDM · beta-phosphoglucomutase from Lactococcus lactis with citrate, tris and acetate bound · 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 0.87

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