MolNFT v1 · #35994 · protein
The crystal structure of the RAS related protein RRAS2 (RRAS2) in the GDP bound state
2ERY · RAS-related protein R-RAS2: “The crystal structure of the RAS related protein RRAS2 (RRAS2) in the GDP bound state”. X-ray diffraction, 2 ligands (GDP, MG), 4 pockets (best druggability 0.46). MolNFT v1 #35994 on GenesisL1: 3D…
- 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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