MolNFT v1 · #148330 · protein
The crystal structure of glycogen phosphorylase in complex with 10A
6F3J · Glycogen phosphorylase, muscle form: “The crystal structure of glycogen phosphorylase in complex with 10A”. X-ray diffraction, 3 ligands (PLP, IMP, CKQ), 11 pockets (best druggability 0.85). MolNFT v1 #148330 on GenesisL1: 3D…
- PDB
- 6F3J
- 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
- PLP, IMP, CKQ
- Pockets
- 11 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen phosphorylase, muscle form (EC 2.4.1.1) | protein | 810 | 53% helix, 16% strand | P00489 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- IMP · Inosinic acid · ligand · chains A
- CKQ · 4-[4-[5-[(2~{S},3~{R},4~{R},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]-4~{H}-1,2,4-triazol-3-yl]phenyl]benzoic acid · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.85 | 0.95 | 53 | PLP, CKQ |
| 2 | 89 | 0.73 | 0.96 | 25 | empty |
| 3 | 50 | 0.70 | 0.98 | 19 | empty |
| 4 | 451 | 0.69 | 0.80 | 64 | empty |
| 5 | 108 | 0.51 | 0.81 | 18 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 6F3J · The crystal structure of Glycogen Phosphorylase in complex with 10a · 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 6F3J · PDBe 6F3J · UniProt P00489
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