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Crystal structures at 2.2 ångströms resolution of the catalytic domains of normal RAS protein and an oncogenic mutant complexed with gsp
Analyse Crystal structures at 2.2 ångströms resolution of the catalytic domains of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q21
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-H-RAS P21 protein catalytic domain
- UniProt
- P01112
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-H-RAS P21 protein catalytic domain | protein | 171 | 34% helix, 25% 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.52 | 0.79 | 37 | MG, GDP |
Compared structures
- 2Q21 · Crystal structures at 2.2 ångströms resolution of the catalytic domains of normal RAS… · 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 2Q21 · PDBe 2Q21 · UniProt P01112
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