MolNFT v1 · #60542 · protein
Tracking structure activity relationships of glycogen phosphorylase inhibitors: synthesis, kinetic and crystallographic evaluation of analogues of N-(-D-glucopyranosyl)-N'-oxamides
3CUV · Glycogen phosphorylase, muscle form: “Tracking structure activity relationships of glycogen phosphorylase inhibitors: synthesis, kinetic and…”. X-ray diffraction, 1 ligand (475), 13 pockets (best druggability 0.81). MolNFT v1 #60542…
- PDB
- 3CUV
- Type
- protein
- Length
- 812 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
- 475
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen phosphorylase, muscle form (EC 2.4.1.1) | protein | 812 | 54% helix, 15% strand | P00489 |
Ligands and binding sites
- 475 · N-[oxo(pyridin-2-ylamino)acetyl]-beta-D-glucopyranosylamine · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · 15 copies · 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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.81 | 0.96 | 35 | 475 |
| 2 | 84 | 0.73 | 0.96 | 26 | empty |
| 3 | 51 | 0.70 | 0.98 | 17 | empty |
| 4 | 332 | 0.70 | 0.83 | 38 | empty |
| 5 | 117 | 0.54 | 0.82 | 19 | empty |
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 3CUV · Tracking structure activity relationships of glycogen phosphorylase inhibitors… · 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 3CUV · PDBe 3CUV · UniProt P00489
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