Research workbench
AlphaFold monomer V2.0 prediction for CAMP/CGMP-dependent 3',5'-CAMP/CGMP phosphodiesterase 7 (Q54HY0)
Analyse AlphaFold monomer V2.0 prediction for CAMP/CGMP-dependent 3',5'-CAMP/CGMP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54HY0
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa3452b8cEc5f7d4aA7eA35d2483a9795B3ae3C17
- Molecule
- CAMP/CGMP-dependent 3',5'-CAMP/CGMP phosphodiesterase 7
- UniProt
- Q54HY0
- Pockets
- 4 · best druggability 0.45
Structure
1 distinct chain · 27% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CAMP/CGMP-dependent 3',5'-CAMP/CGMP phosphodiesterase 7 | protein | 425 | 27% helix, 21% strand | Q54HY0 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.45 | 0.76 | 28 | empty |
| 2 | 75 | 0.38 | 0.78 | 18 | empty |
| 3 | 63 | 0.32 | 0.75 | 19 | empty |
| 4 | 50 | 0.27 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q54HY0
- Elsewhere: UniProt Q54HY0 · AlphaFold DB Q54HY0
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