Research workbench
The crystal structure of glycogen phosphorylase in complex with 10C
Analyse The crystal structure of glycogen phosphorylase in complex with 10C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F3R
- 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, CKZ
- Pockets
- 10 · 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 | 810 | 53% helix, 15% strand | P00489 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- CKZ · (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[5-(9~{H}-fluoren-2-yl)-4~{H}-1,2,4-triazol-3-yl]-6-(hydroxymethyl)oxane-3,4,5-triol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 348 | 0.86 | 0.95 | 54 | PLP, CKZ |
| 2 | 137 | 0.79 | 0.96 | 39 | empty |
| 3 | 459 | 0.68 | 0.80 | 64 | empty |
| 4 | 258 | 0.54 | 0.76 | 27 | empty |
| 5 | 108 | 0.52 | 0.82 | 19 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 6F3R · The crystal structure of Glycogen Phosphorylase in complex with 10c · 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 6F3R · PDBe 6F3R · UniProt P00489
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