Research workbench
RAS:SOS:RAS in complex with a small molecule activator
Analyse RAS:SOS:RAS in complex with a small molecule activator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CUO
- Type
- protein
- Length
- 802 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase HRAS; Son of sevenless homolog 1
- UniProt
- P01112, Q07889
- Ligands
- GNP, FFS, MG, NA
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase HRAS | protein | 166 | 38% helix, 27% strand | P01112 |
| B | Son of sevenless homolog 1 | protein | 469 | 59% helix, 4% strand | Q07889 |
| C | GTPase HRAS | protein | 167 | 34% helix, 25% strand | P01112 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- FFS · N~2~-(3-chlorophenyl)-N~4~-[(furan-2-yl) methyl]quinazoline-2,4-diamine · ligand · chains B
- MG · Magnesium ion · metal · chains A
- NA · Sodium ion · metal · chains C
- FMT · Formic acid · additive · 6 copies · chains A, B, C
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.80 | 0.82 | 97 | GNP, MG |
| 2 | 263 | 0.72 | 0.86 | 49 | empty |
| 3 | 52 | 0.66 | 0.96 | 17 | empty |
| 4 | 270 | 0.62 | 0.81 | 45 | empty |
| 5 | 98 | 0.59 | 0.86 | 17 | FFS |
Interfaces
2 interfaces between chains.
- B–C · 1796 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1570 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
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 P01112
- Every structure of UniProt Q07889
- Elsewhere: RCSB PDB 6CUO · PDBe 6CUO · UniProt P01112 · UniProt Q07889
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