Research workbench
Crystal structure of rock 1 bound to fasudil
Analyse Crystal structure of rock 1 bound to fasudil in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ESM
- Type
- protein
- Length
- 798 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho-associated protein kinase 1
- EC
- 2.7.1.37
- UniProt
- Q13464
- Ligands
- M77
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-associated protein kinase 1 (EC 2.7.1.37) | protein | 400 | 40% helix, 13% strand | Q13464 |
| B | Rho-associated protein kinase 1 (EC 2.7.1.37) | protein | 398 | 40% helix, 13% strand | Q13464 |
Ligands and binding sites
- M77 · 5-(1,4-diazepan-1-sulfonyl)isoquinoline · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.72 | 0.81 | 54 | M77 |
| 2 | 390 | 0.66 | 0.80 | 48 | M77 |
| 3 | 208 | 0.62 | 0.82 | 33 | empty |
| 4 | 142 | 0.49 | 0.79 | 28 | empty |
| 5 | 50 | 0.45 | 0.85 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2247 Ų buried · 36 hydrogen bonds · protein-protein
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 Q13464
- Elsewhere: RCSB PDB 2ESM · PDBe 2ESM · UniProt Q13464
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.