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Glycogen phosphorylase B in complex with N-4-hydroxybenzoyl-N'-4-beta- D-glucopyranosyl urea

Analyse Glycogen phosphorylase B in complex with N-4-hydroxybenzoyl-N'-4-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QN7
Type
protein
Length
805 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycogen phosphorylase, muscle form
EC
2.4.1.1
UniProt
P00489
Ligands
PLP, HBZ, IMP
Pockets
14 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycogen phosphorylase, muscle form (EC 2.4.1.1)protein80553% helix, 15% strandP00489

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · chains A
  • HBZ · N-{[(4-hydroxyphenyl)carbonyl]carbamoyl}-beta-D-glucopyranosylamine · ligand · chains A
  • IMP · Inosinic acid · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14910.860.9370PLP, HBZ
2920.720.9429empty
34620.700.8150empty
4510.690.9818empty
51130.530.8218empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 2QN7 · Glycogen Phosphorylase b in complex with N-4-hydroxybenzoyl-N'-4-beta-D-glucopyranosyl… · the same entry in another collection · chain A against A, TM-score 1.00

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