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A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe.

Analyse A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MEM
Type
protein
Length
807 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, 7LS
Pockets
12 · best druggability 0.85

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycogen phosphorylase, muscle form (EC 2.4.1.1)protein80753% helix, 15% strandP00489

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · chains A
  • 7LS · 2-[[1-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]-2-oxidanylidene-pyrimidin-4-yl]amino]-10~{H}-acridin-9-one · ligand · 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, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13170.850.9551PLP, 7LS
25620.760.8379empty
32020.520.7720empty
41070.520.8223empty
5950.500.8217empty

Modifications

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

Compared structures

  • 5MEM · A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe. · the same entry in another collection · chain A against A, TM-score 1.00

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