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Beta-phosphoglucomutase from lactococcus lactis with inorganic phosphate bound in an open conformer to 1.8 a.

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

PDB
6H93
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, PO4
Pockets
2 · best druggability 0.73

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
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
  • ACT · Acetate ion · additive · 2 copies · chains A
  • PDO · 1,3-propandiol · additive · chains A

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
14680.730.8352MG, EDO, PO4
24670.690.8048EDO, ACT, PO4

Interfaces

1 interface between chains.

  • A–B · 570 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6H93 · Beta-phosphoglucomutase from Lactococcus lactis with inorganic phosphate bound in an open… · 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

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