Research workbench
Crystal structure of PDE6D Geranylgeranylated cystein complex
Analyse Crystal structure of PDE6D Geranylgeranylated cystein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q9Q
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.45
- Source
- Homo sapiens
- Molecule
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- UniProt
- O43924
- Ligands
- CMT, GER
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · resolution 1.45 · 1 distinct chain · 14% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| BBB | Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta | protein | 148 | 14% helix, 59% strand | O43924 |
Ligands and binding sites
- CMT · O-methylcysteine · ligand · chains BBB
- GER · Geran-8-yl geran · ligand · chains BBB
- EDO · 1,2-ethanediol · additive · 3 copies · chains BBB
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 421 | 0.82 | 0.89 | 43 | CMT, GER |
Compared structures
- O43924 · AlphaFold monomer V2.0 prediction for retinal rod rhodopsin-sensitive cgmp 3',5'-cyclic… · a predicted model of the same protein · chain BBB against A, TM-score 0.97
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 O43924
- Elsewhere: RCSB PDB 7Q9Q · PDBe 7Q9Q · UniProt O43924
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