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MolNFT v1 · #6419 · protein

Human liver glycogen phosphorylase complexed with N-acetyl-beta-D- glucopyranosylamine

1FC0 · Glycogen phosphorylase, liver form: “Human liver glycogen phosphorylase complexed with N-acetyl-beta-D- glucopyranosylamine”. X-ray diffraction, 2 ligands (NBG, PLP), 20 pockets (best druggability 0.86). MolNFT v1 #6419 on…

PDB
1FC0
Type
protein
Length
1,585 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycogen phosphorylase, liver form
EC
2.4.1.1
UniProt
P06737
Ligands
NBG, PLP
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycogen phosphorylase, liver form (EC 2.4.1.1)protein79253% helix, 16% strandP06737
BGlycogen phosphorylase, liver form (EC 2.4.1.1)protein79353% helix, 16% strandP06737

Ligands and binding sites

  • NBG · N-acetyl-beta-D-glucopyranosylamine · ligand · 2 copies · chains A, B
  • PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111260.860.8776empty
23060.850.9655NBG, PLP
33000.840.9551NBG, PLP
41200.780.9738empty
5900.720.9428empty

Interfaces

1 interface between chains.

  • A–B · 2239 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 1FC0 · Human liver glycogen phosphorylase complexed with N-acetyl-beta-D-glucopyranosylamine · the same entry in another collection · chain A against A, TM-score 1.00
  • P06737 · AlphaFold monomer V2.0 prediction for glycogen phosphorylase, liver form (P06737) · a predicted model of the same protein · chain A against A, TM-score 0.99

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