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Crystal structure of the R503Q missense variant of human PGM1

Analyse Crystal structure of the R503Q missense variant of human PGM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VG7
Type
protein
Length
1,126 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphoglucomutase-1
EC
5.4.2.2
UniProt
P36871
Ligands
MG, SO4
Pockets
10 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphoglucomutase-1 (EC 5.4.2.2)protein56437% helix, 26% strandP36871
BPhosphoglucomutase-1 (EC 5.4.2.2)protein56236% helix, 26% strandP36871

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 18 copies · chains A, B
  • GOL · Glycerol · additive · 5 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15440.670.7860SO4, GOL
26380.660.7665SO4, GOL
36190.660.7664SO4
41380.480.7827GOL
51430.440.7525empty

Interfaces

1 interface between chains.

  • A–B · 521 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 5VG7 · Crystal Structure of the R503Q missense variant of human PGM1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P36871 · AlphaFold monomer V2.0 prediction for phosphoglucomutase-1 (P36871) · a predicted model of the same protein · chain B against A, TM-score 0.99

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