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Crystal structure of mouse rhoa-GTP complex
Analyse Crystal structure of mouse rhoa-GTP complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TVD
- Type
- protein
- Length
- 360 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein rhoa
- UniProt
- P61589
- Ligands
- GSP, MG
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transforming protein rhoa | protein | 180 | 40% helix, 24% strand | P61589 |
Ligands and binding sites
- GSP · 5'-guanosine-diphosphate-monothiophosphate · 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 | 116 | 0.46 | 0.79 | 22 | empty |
| 2 | 128 | 0.45 | 0.77 | 30 | GSP, MG |
| 3 | 106 | 0.42 | 0.77 | 27 | GSP, MG |
| 4 | 55 | 0.30 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 528 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 P61589
- Elsewhere: RCSB PDB 3TVD · PDBe 3TVD · UniProt P61589
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