Research workbench
PDE2 catalytic domain complexed with inhibitors
Analyse PDE2 catalytic domain complexed with inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U7J
- Type
- protein
- Length
- 1,328 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cgmp-dependent 3',5'-cyclic phosphodiesterase
- EC
- 3.1.4.17
- UniProt
- O00408
- Ligands
- 7XV, ZN, MG
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cgmp-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) | protein | 338 | 69% helix, 0% strand | O00408 |
| B | Cgmp-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) | protein | 336 | 69% helix, 0% strand | O00408 |
| C, D | Cgmp-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) | protein | 327 | 69% helix, 0% strand | O00408 |
Ligands and binding sites
- 7XV · 5-[2-(2-methoxyphenyl)ethoxy]-3-(2-methylpropyl)[1,2, 4]triazolo[4,3-a]pyrazine · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 907 | 0.82 | 0.84 | 70 | 7XV, MG |
| 2 | 406 | 0.73 | 0.84 | 41 | 7XV, MG |
| 3 | 383 | 0.72 | 0.83 | 40 | 7XV, MG |
| 4 | 384 | 0.72 | 0.83 | 42 | 7XV, MG |
| 5 | 554 | 0.71 | 0.80 | 56 | empty |
Interfaces
5 interfaces between chains.
- C–D · 899 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 802 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 735 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 420 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 90 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5U7J · PDE2 catalytic domain complexed with 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 O00408
- Elsewhere: RCSB PDB 5U7J · PDBe 5U7J · UniProt O00408
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.