MolNFT v1 · #182509 · protein
Rhodopsin kinase (GRK1)-S5E/S488E/T489E in complex with rhodopsin
7MT8 · Rhodopsin kinase GRK1: “Rhodopsin kinase (GRK1)-S5E/S488E/T489E in complex with rhodopsin”. Electron microscopy, 2 ligands (SGV, RET), 6 pockets (best druggability 0.86). MolNFT v1 #182509 on GenesisL1: 3D structure, binding sites…
- PDB
- 7MT8
- Type
- protein
- Length
- 670 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhodopsin kinase GRK1; Rhodopsin
- EC
- 2.7.11.14
- UniProt
- P28327, P02699
- Ligands
- SGV, RET
- Pockets
- 6 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 52% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G | Rhodopsin kinase GRK1 (EC 2.7.11.14) | protein | 346 | 38% helix, 14% strand | P28327 |
| R | Rhodopsin | protein | 324 | 68% helix, 3% strand | P02699 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.86 | 0.94 | 53 | empty |
| 2 | 227 | 0.85 | 0.97 | 26 | RET |
| 3 | 528 | 0.77 | 0.84 | 54 | SGV |
| 4 | 135 | 0.46 | 0.77 | 20 | empty |
| 5 | 63 | 0.35 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- G–R · 1861 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor, 1 disulfide (retinal Schiff base, disulfide).
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
- Every structure of UniProt P02699
- Elsewhere: RCSB PDB 7MT8 · PDBe 7MT8 · UniProt P28327 · UniProt P02699
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