Research workbench
The crystal structure of the RAS related protein RRAS2 (RRAS2) in the GDP bound state
Analyse The crystal structure of the RAS related protein RRAS2 (RRAS2) in the GDP bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ERY
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related protein R-RAS2
- UniProt
- P62070
- Ligands
- GDP, MG
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein R-RAS2 | protein | 167 | 37% helix, 27% strand | P62070 |
| B | RAS-related protein R-RAS2 | protein | 169 | 35% helix, 28% strand | P62070 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · 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
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.46 | 0.77 | 33 | empty |
| 2 | 117 | 0.43 | 0.77 | 28 | MG, GDP |
| 3 | 114 | 0.43 | 0.77 | 25 | MG, GDP |
| 4 | 130 | 0.40 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 391 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2ERY · The crystal structure of the Ras related protein RRas2 (RRAS2) in the GDP bound state · the same entry in another collection · chain A against A, TM-score 1.00
- P62070 · AlphaFold monomer V2.0 prediction for RAS-related protein R-RAS2 (P62070) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P62070
- Elsewhere: RCSB PDB 2ERY · PDBe 2ERY · UniProt P62070
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