Research workbench
The crystal structure of the human RAC3 in complex with GDP and chloride
Analyse The crystal structure of the human RAC3 in complex with GDP and chloride in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G0N
- Type
- protein
- Length
- 357 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related C3 botulinum toxin substrate 3
- UniProt
- P60763
- Ligands
- GDP, MG, CL
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related C3 botulinum toxin substrate 3 | protein | 179 | 39% helix, 23% strand | P60763 |
| B | RAS-related C3 botulinum toxin substrate 3 | protein | 178 | 39% helix, 24% strand | P60763 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
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 | 1031 | 0.79 | 0.81 | 83 | MG, CL, GDP |
Interfaces
1 interface between chains.
- A–B · 842 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2G0N · The Crystal Structure of the Human RAC3 in complex with GDP and Chloride · the same entry in another collection · chain A against A, TM-score 1.00
- P60763 · AlphaFold monomer V2.0 prediction for RAS-related C3 botulinum toxin substrate 3 (P60763) · 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 P60763
- Elsewhere: RCSB PDB 2G0N · PDBe 2G0N · UniProt P60763
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