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The crystal structure of glycogen phosphorylase in complex with 14

Analyse The crystal structure of glycogen phosphorylase in complex with 14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S52
Type
protein
Length
810 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
KVN, PLP
Pockets
11 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycogen phosphorylase, muscle form (EC 2.4.1.1)protein81053% helix, 16% strandP00489

Ligands and binding sites

  • KVN · (2~{R},3~{S},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-(5-phenyl-1,2,3,4-tetrazol-2-yl)oxane-3,4,5-triol · ligand · chains A
  • PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12820.850.9649KVN, PLP
2780.730.9626empty
34220.680.8060empty
41280.540.8219empty
51960.510.7724empty

Modifications

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

Compared structures

  • 6S52 · The crystal structure of glycogen phosphorylase in complex with 14 · the same entry in another collection · chain A against A, TM-score 1.00

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