Research workbench
Glycogen phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D- glucopyranosyl urea
Analyse Glycogen phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QN9
- 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, NBX, IMP
- Pockets
- 14 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen phosphorylase, muscle form (EC 2.4.1.1) | protein | 807 | 53% helix, 15% strand | P00489 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- NBX · N-{[(4-aminophenyl)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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 493 | 0.86 | 0.93 | 66 | PLP, NBX |
| 2 | 86 | 0.71 | 0.94 | 29 | empty |
| 3 | 51 | 0.69 | 0.98 | 17 | empty |
| 4 | 289 | 0.68 | 0.83 | 34 | empty |
| 5 | 124 | 0.53 | 0.81 | 18 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2QN9 · Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea · 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 2QN9 · PDBe 2QN9 · UniProt P00489
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