Research workbench
Rhodopsin kinase (GRK1) L166K mutant at 2.5A resolution
Analyse Rhodopsin kinase (GRK1) L166K mutant at 2.5A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T8O
- Type
- protein
- Length
- 493 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhodopsin kinase
- EC
- 2.7.11.14
- UniProt
- P28327
- Ligands
- ATP, MG, CL
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhodopsin kinase (EC 2.7.11.14) | protein | 493 | 46% helix, 12% strand | P28327 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.66 | 0.78 | 42 | ATP, MG |
| 2 | 133 | 0.54 | 0.81 | 22 | empty |
| 3 | 182 | 0.49 | 0.77 | 32 | empty |
| 4 | 51 | 0.22 | 0.71 | 14 | empty |
Compared structures
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 P28327
- Elsewhere: RCSB PDB 3T8O · PDBe 3T8O · UniProt P28327
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