Research workbench
Structure of the Q61G mutant of RAS in the GDP-bound form
Analyse Structure of the Q61G mutant of RAS in the GDP-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZVQ
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein P21/H-RAS-1
- UniProt
- P01112
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein P21/H-RAS-1 | protein | 166 | 37% helix, 26% strand | P01112 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.46 | 0.78 | 25 | MG, GDP |
Compared structures
- 1ZVQ · Structure of the Q61G mutant of Ras in the GDP-bound form · 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 P01112
- Elsewhere: RCSB PDB 1ZVQ · PDBe 1ZVQ · UniProt P01112
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