Research workbench
Structure of a photoactivatable RAC1 containing LOV2 wildtype
Analyse Structure of a photoactivatable RAC1 containing LOV2 wildtype in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WKP
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NPH1-1, RAS-related C3 botulinum toxin substrate 1
- UniProt
- O49003, P63000
- Ligands
- GTP, FMN, MG, CA
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NPH1-1, RAS-related C3 botulinum toxin substrate 1 | protein | 320 | 38% helix, 26% strand | O49003, P63000 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.70 | 0.88 | 25 | FMN |
| 2 | 185 | 0.56 | 0.80 | 39 | GTP, MG |
| 3 | 106 | 0.38 | 0.75 | 18 | empty |
| 4 | 75 | 0.34 | 0.75 | 13 | empty |
Compared structures
- 2WKP · Structure of a photoactivatable Rac1 containing Lov2 Wildtype · the same entry in another collection · chain A against A, TM-score 1.00
- P63000 · AlphaFold monomer V2.0 prediction for RAS-related C3 botulinum toxin substrate 1 (P63000) · a predicted model of the same protein · chain A against A, TM-score 0.56
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 O49003
- Every structure of UniProt P63000
- Elsewhere: RCSB PDB 2WKP · PDBe 2WKP · UniProt O49003 · UniProt P63000
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