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Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the inhibitor and the allosteric site. broad specificities of the two sites
Analyse Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z62
- 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
- IAA, PLP
- Pockets
- 13 · best druggability 0.85
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 | 809 | 53% helix, 15% strand | P00489 |
Ligands and binding sites
- IAA · ({[(3E)-2'-oxo-2',7'-dihydro-2,3'-biindol-3(7H)-ylidene]amino}oxy)acetic acid · ligand · 3 copies · chains A
- PLP · Pyridoxal-5'-phosphate · ligand · 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.85 | 0.96 | 56 | PLP |
| 2 | 86 | 0.71 | 0.95 | 27 | empty |
| 3 | 460 | 0.71 | 0.81 | 58 | empty |
| 4 | 112 | 0.53 | 0.82 | 18 | empty |
| 5 | 196 | 0.51 | 0.77 | 19 | IAA |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1Z62 · Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the inhibitor… · 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 1Z62 · PDBe 1Z62 · UniProt P00489
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