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CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 10 IN COMPLEX WITH N4(c1nn(c(n1)CCc3nn2c(cnc(C)c2n3)C)C)C[C@H](F)CC4, micromolar IC50=0.010653
Analyse CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 10 IN COMPLEX WITH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SH9
- Type
- protein
- Length
- 1,254 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.06
- Source
- Homo sapiens
- Molecule
- cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
- EC
- 3.1.4.17
- UniProt
- Q9Y233
- Ligands
- JAP, ZN, MG
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · resolution 2.06 · 3 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) | protein | 313 | 71% helix, 0% strand | Q9Y233 |
| B | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) | protein | 316 | 71% helix, 0% strand | Q9Y233 |
| D | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) | protein | 312 | 71% helix, 0% strand | Q9Y233 |
Ligands and binding sites
- JAP · (4S)-2-(2-{3-[(3R)-3-fluoropyrrolidin-1-yl]-1-methyl-1H-1,2,4-triazol-5-yl}ethyl)-5,8-dimethyl[1,2,4]triazolo[1,5-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
- PG4 · Tetraethylene glycol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.73 | 0.83 | 50 | MG, JAP |
| 2 | 690 | 0.73 | 0.80 | 66 | empty |
| 3 | 440 | 0.73 | 0.83 | 51 | MG, JAP |
| 4 | 415 | 0.72 | 0.82 | 48 | MG, JAP |
| 5 | 411 | 0.71 | 0.82 | 48 | MG, JAP |
Interfaces
5 interfaces between chains.
- A–C · 729 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 703 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 695 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 520 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 58 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 4 modified (disulfide, artifact).
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 Q9Y233
- Elsewhere: RCSB PDB 5SH9 · PDBe 5SH9 · UniProt Q9Y233
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