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Crystal structure of the D263G missense variant of human PGM1

Analyse Crystal structure of the D263G 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
5TR2
Type
protein
Length
1,113 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
CA, SO4
Pockets
12 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphoglucomutase-1 (EC 5.4.2.2)protein56136% helix, 25% strandP36871
BPhosphoglucomutase-1 (EC 5.4.2.2)protein55236% helix, 24% strandP36871

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 4 copies · chains A, B
  • GOL · Glycerol · additive · chains A

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

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17230.720.7873SO4, GOL
25000.650.7860SO4
3640.630.9122empty
43480.580.7646empty
51220.570.8433empty

Interfaces

1 interface between chains.

  • A–B · 141 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 5TR2 · Crystal structure of the D263G 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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