GL1X · GenesisL1 explorer

Research workbench

Complex of the enzyme PMM/PGM with xylose 1-phosphate

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

PDB
2H5A
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
X1P, ZN
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XPHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE (EC 5.4.2.8, 5.4.2.2)protein45538% helix, 24% strandP26276

Ligands and binding sites

  • X1P · 1-O-phosphono-alpha-D-xylopyranose · 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14580.720.8270X1P
21240.500.7918empty
3810.350.7618empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 2H5A · Complex of the enzyme PMM/PGM with xylose 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

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.