Research workbench
Crystal structure of photoinhibitable RAC1 containing C450A mutant LOV2 domain
Analyse Crystal structure of photoinhibitable RAC1 containing C450A mutant LOV2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HZH
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related C3 botulinum toxin substrate 1,NPH1-1,RAS- related C3 botulinum toxin…
- UniProt
- P63000, O49003
- Ligands
- GTP, FMN, CA, MG
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related C3 botulinum toxin substrate 1,NPH1-1,RAS- related C3 botulinum toxin substrate 1 | protein | 320 | 38% helix, 25% strand | P63000, O49003 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
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 | 190 | 0.70 | 0.88 | 24 | FMN |
| 2 | 126 | 0.53 | 0.81 | 33 | GTP, MG |
| 3 | 97 | 0.46 | 0.80 | 19 | empty |
Compared structures
- 5HZH · Crystal structure of photoinhibitable Rac1 containing C450A mutant LOV2 domain · 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
- Every structure of UniProt O49003
- Elsewhere: RCSB PDB 5HZH · PDBe 5HZH · UniProt P63000 · UniProt O49003
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