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Complex of PMM/PGM with ribose 1-phosphate

Analyse Complex of PMM/PGM with ribose 1-phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2H4L
Type
protein
Length
455 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE
EC
5.4.2.8, 5.4.2.2
UniProt
P26276
Ligands
R1P, ZN
Pockets
4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XPHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE (EC 5.4.2.8, 5.4.2.2)protein45537% helix, 25% strandP26276

Ligands and binding sites

  • R1P · 1-O-phosphono-alpha-D-ribofuranose · ligand · chains X
  • ZN · Zinc ion · metal · chains X

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13740.680.8157R1P
21170.490.8018empty
31140.380.7422empty
4750.350.7618empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 2H4L · Complex of PMM/PGM with ribose 1-phosphate · the same entry in another collection · chain X against X, TM-score 1.00
  • P26276 · AlphaFold monomer V2.0 prediction for PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE (P26276) · a predicted model of the same protein · chain X against A, TM-score 1.00

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