Research workbench
Rho-associated protein kinase 1 (rock 1) in complex with a pyridine thiazole piperidine inhibitor
Analyse Rho-associated protein kinase 1 (rock 1) in complex with a pyridine thiazole… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HVU
- Type
- protein
- Length
- 788 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
- 65R
- Pockets
- 14 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 394 | 40% helix, 14% strand | Q13464 |
| B | Rho-associated protein kinase 1 (EC 2.7.11.1) | protein | 394 | 40% helix, 14% strand | Q13464 |
Ligands and binding sites
- 65R · 2-{3-[3-(piperidin-4-yl)propoxy]phenyl}-N-[4-(pyridin-4-yl)-1,3-thiazol-2-yl]acetamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 398 | 0.67 | 0.80 | 42 | 65R |
| 2 | 384 | 0.66 | 0.79 | 39 | 65R |
| 3 | 279 | 0.65 | 0.82 | 32 | empty |
| 4 | 50 | 0.47 | 0.86 | 17 | empty |
| 5 | 73 | 0.44 | 0.81 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2248 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 5HVU · Rho-associated protein kinase 1 (ROCK 1) in complex with a pyridine thiazole piperidine… · the same entry in another collection · chain A against A, TM-score 1.00
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 5HVU · PDBe 5HVU · UniProt Q13464
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