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X-ray co-structure of rho-associated protein kinase (ROCK1) with a highly selective inhibitor
Analyse X-ray co-structure of rho-associated protein kinase (ROCK1) with a highly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WNE
- Type
- protein
- Length
- 1,516 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13464
- Ligands
- B4J
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 384 | — | Q13464 |
| B | — | protein | 352 | — | Q13464 |
| C | — | protein | 384 | — | Q13464 |
| D | — | protein | 396 | — | Q13464 |
Ligands and binding sites
- B4J · 3,4-dimethoxy-N-({3-[(5-methyl-4,5,6,7-tetrahydro[1, 3]thiazolo[5,4-c]pyridin-2-yl) carbamoyl]phenyl}methyl)benzamide · ligand · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WNE · X-ray co-structure of rho-associated protein kinase (ROCK1) with a highly selective… · 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 5WNE · PDBe 5WNE · UniProt Q13464
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