MolNFT v1 · #61041 · protein
Crystal structure of rock I bound to H-1152P a di- methylated variant of fasudil
3D9V · Rho-associated protein kinase 1: “Crystal structure of rock I bound to H-1152P a di- methylated variant of fasudil”. X-ray diffraction, 1 ligand (H52), 15 pockets (best druggability 0.71). MolNFT v1 #61041 on GenesisL1: 3D…
- PDB
- 3D9V
- 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
- 2.7.11.1
- UniProt
- Q13464
- Ligands
- H52
- Pockets
- 15 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 400 | 38% helix, 14% strand | Q13464 |
| B | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 398 | 37% helix, 14% strand | Q13464 |
Ligands and binding sites
- H52 · (S)-2-methyl-1-[(4-methyl-5-isoquinoline)sulfonyl]-homopiperazine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 529 | 0.71 | 0.80 | 50 | H52 |
| 2 | 382 | 0.67 | 0.80 | 40 | H52 |
| 3 | 254 | 0.64 | 0.82 | 36 | empty |
| 4 | 82 | 0.55 | 0.86 | 21 | empty |
| 5 | 103 | 0.48 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2256 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 3D9V · Crystal structure of rock I bound to H-1152P a di-methylated variant of fasudil · the same entry in another collection · chain A against A, TM-score 1.00
- Q13464 · AlphaFold monomer V2.0 prediction for rho-associated protein kinase 1 (Q13464) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 3D9V · PDBe 3D9V · UniProt Q13464
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.