Research workbench
Crystal structure of the catalytic domain of rat phosphodiesterase 10A
Analyse Crystal structure of the catalytic domain of rat phosphodiesterase 10A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OVV
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphodiesterase-10A
- EC
- 3.1.4.17
- UniProt
- Q9QYJ6
- Ligands
- PFH, ZN, MG, SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphodiesterase-10A (EC 3.1.4.17) | protein | 304 | 72% helix, 0% strand | Q9QYJ6 |
Ligands and binding sites
- PFH · 6,7-dimethoxy-4-[(3R)-3-(2-naphthyloxy)pyrrolidin-1-yl]quinazoline · ligand · chains A
- ZN · Zinc ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 422 | 0.72 | 0.83 | 48 | MG, PFH |
| 2 | 109 | 0.52 | 0.82 | 20 | empty |
| 3 | 57 | 0.31 | 0.76 | 14 | empty |
Compared structures
- 2OVV · Crystal structure of the catalytic domain of rat phosphodiesterase 10A · the same entry in another collection · chain A against A, TM-score 1.00
- Q9QYJ6 · AlphaFold monomer V2.0 prediction for camp and camp-inhibited cgmp 3',5'-cyclic… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9QYJ6
- Elsewhere: RCSB PDB 2OVV · PDBe 2OVV · UniProt Q9QYJ6
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