Research workbench
Coiled-coil structure of the rhoa-binding domain in rho- kinase
Analyse Coiled-coil structure of the rhoa-binding domain in rho- kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UIX
- Type
- protein
- Length
- 137 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho-associated kinase
- EC
- 2.7.1.-
- UniProt
- Q28021
Structure
x-ray diffraction · 2 distinct chains · 96% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-associated kinase (EC 2.7.1.-) | protein | 69 | 96% helix, 0% strand | Q28021 |
| B | Rho-associated kinase (EC 2.7.1.-) | protein | 68 | 96% helix, 0% strand | Q28021 |
Interfaces
1 interface between chains.
- A–B · 1527 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 1UIX · Coiled-coil structure of the RhoA-binding domain in Rho-kinase · the same entry in another collection · chain A against A, TM-score 1.00
- Q28021 · AlphaFold monomer V2.0 prediction for rho-associated protein kinase 2 (Q28021) · a predicted model of the same protein · chain B against A, TM-score 0.91
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 Q28021
- Elsewhere: RCSB PDB 1UIX · PDBe 1UIX · UniProt Q28021
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.