MolNFT v1 · #163495 · protein
The crystal structure of glycogen phosphorylase in complex with 9
6S4O · Glycogen phosphorylase, muscle form: “The crystal structure of glycogen phosphorylase in complex with 9”. X-ray diffraction, 3 ligands (KV5, PLP, IMP), 14 pockets (best druggability 0.85). MolNFT v1 #163495 on GenesisL1: 3D…
- PDB
- 6S4O
- Type
- protein
- Length
- 809 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
- KV5, PLP, IMP
- Pockets
- 14 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen phosphorylase, muscle form (EC 2.4.1.1) | protein | 809 | 52% helix, 16% strand | P00489 |
Ligands and binding sites
- KV5 · (2~{R},3~{S},4~{R},5~{R},6~{S})-2-(hydroxymethyl)-6-(2-naphthalen-2-yl-1~{H}-imidazol-4-yl)oxane-3,4,5-triol · ligand · chains A
- PLP · Pyridoxal-5'-phosphate · 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 303 | 0.85 | 0.95 | 47 | KV5, PLP |
| 2 | 80 | 0.71 | 0.95 | 28 | empty |
| 3 | 413 | 0.69 | 0.81 | 56 | empty |
| 4 | 196 | 0.51 | 0.77 | 27 | IMP |
| 5 | 95 | 0.50 | 0.82 | 21 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 6S4O · The crystal structure of glycogen phosphorylase in complex with 9 · 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 6S4O · PDBe 6S4O · UniProt P00489
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