Research workbench
Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site
Analyse Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E1Y
- Type
- protein
- Length
- 813 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
- CPB, PLP, GLC, PO3
- Pockets
- 13 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen phosphorylase, muscle form (EC 2.4.1.1) | protein | 813 | 52% helix, 15% strand | P00489 |
Ligands and binding sites
- CPB · 2-(2-chloro-phenyl)-5,7-dihydroxy-8-(3-hydroxy-1-methyl-piperidin-4-yl)-4H-benzopyran-4-one · ligand · chains A
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- PO3 · Phosphite ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.85 | 0.96 | 48 | GLC, PLP |
| 2 | 201 | 0.77 | 0.92 | 43 | empty |
| 3 | 533 | 0.67 | 0.78 | 63 | empty |
| 4 | 108 | 0.52 | 0.82 | 19 | empty |
| 5 | 117 | 0.51 | 0.81 | 31 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1E1Y · Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00489
- Elsewhere: RCSB PDB 1E1Y · PDBe 1E1Y · UniProt P00489
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