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Crystal structure of RAC1 P29S mutant
Analyse Crystal structure of RAC1 P29S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SBD
- Type
- protein
- Length
- 353 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related C3 botulinum toxin substrate 1
- UniProt
- P63000
- Ligands
- GNP, MG
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related C3 botulinum toxin substrate 1 | protein | 177 | 38% helix, 26% strand | P63000 |
| B | RAS-related C3 botulinum toxin substrate 1 | protein | 176 | 38% helix, 26% strand | P63000 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · 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
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.59 | 0.82 | 30 | GNP, MG |
| 2 | 180 | 0.57 | 0.81 | 32 | GNP, MG |
| 3 | 65 | 0.30 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 476 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3SBD · Crystal structure of RAC1 P29S mutant · 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 P63000
- Elsewhere: RCSB PDB 3SBD · PDBe 3SBD · UniProt P63000
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