Research workbench
Crystal structure of the complex between the human rhoa and rho-binding domain of human rocki
Analyse Crystal structure of the complex between the human rhoa and rho-binding domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S1C
- Type
- protein
- Length
- 497 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein rhoa; Rho-associated, coiled-coil containing protein kinase 1
- UniProt
- P61586, Q13464
- Ligands
- GNP, MG
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 61% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transforming protein rhoa | protein | 179 | 40% helix, 26% strand | P61586 |
| X | Rho-associated, coiled-coil containing protein kinase 1 | protein | 69 | 93% helix, 0% strand | Q13464 |
| Y | Rho-associated, coiled-coil containing protein kinase 1 | protein | 70 | 86% helix, 0% strand | Q13464 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.56 | 0.78 | 39 | MG, GNP |
| 2 | 197 | 0.55 | 0.79 | 34 | MG, GNP |
| 3 | 57 | 0.33 | 0.76 | 11 | empty |
Interfaces
5 interfaces between chains.
- X–Y · 1596 Ų buried · 13 hydrogen bonds · protein-protein
- A–Y · 406 Ų buried · 2 hydrogen bonds · protein-protein
- B–Y · 355 Ų buried · 3 hydrogen bonds · protein-protein
- A–X · 353 Ų buried · 4 hydrogen bonds · protein-protein
- B–X · 339 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1S1C · Crystal structure of the complex between the human RhoA and Rho-binding domain of human… · the same entry in another collection · chain A against A, TM-score 1.00
- P61586 · AlphaFold monomer V2.0 prediction for transforming protein rhoa (P61586) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q13464 · AlphaFold monomer V2.0 prediction for rho-associated protein kinase 1 (Q13464) · a predicted model of the same protein · chain Y against A, TM-score 0.79
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 P61586
- Every structure of UniProt Q13464
- Elsewhere: RCSB PDB 1S1C · PDBe 1S1C · UniProt P61586 · UniProt Q13464
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