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Crystal structure of the C-terminal gaf domain of human phosphodiesterase 10A
Analyse Crystal structure of the C-terminal gaf domain of human phosphodiesterase 10A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZMF
- Type
- protein
- Length
- 349 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp and camp-inhibited cgmp 3',5'-cyclic phosphodiesterase 10A
- EC
- 3.1.4.17
- UniProt
- Q9Y233
- Ligands
- CMP
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp and camp-inhibited cgmp 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) | protein | 177 | 42% helix, 27% strand | Q9Y233 |
| B | Camp and camp-inhibited cgmp 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) | protein | 172 | 40% helix, 30% strand | Q9Y233 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.78 | 0.97 | 23 | CMP |
| 2 | 103 | 0.78 | 0.97 | 22 | CMP |
| 3 | 374 | 0.62 | 0.77 | 36 | empty |
| 4 | 118 | 0.38 | 0.74 | 21 | empty |
| 5 | 61 | 0.36 | 0.78 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1559 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2ZMF · Crystal structure of the C-terminal GAF domain of human phosphodiesterase 10A · 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 Q9Y233
- Elsewhere: RCSB PDB 2ZMF · PDBe 2ZMF · UniProt Q9Y233
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