Research workbench
Shigella IPGB2 in complex with human rhoa and GDP (complex C)
Analyse Shigella IPGB2 in complex with human rhoa and GDP (complex C) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LXR
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein rhoa; IPGB2
- UniProt
- P61586, Q9AJW7
- Ligands
- GDP, SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein rhoa | protein | 180 | 38% helix, 23% strand | P61586 |
| F | IPGB2 | protein | 181 | 63% helix, 13% strand | Q9AJW7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.72 | 0.86 | 43 | empty |
| 2 | 477 | 0.61 | 0.75 | 47 | empty |
| 3 | 299 | 0.57 | 0.77 | 37 | GDP |
Interfaces
1 interface between chains.
- A–F · 1416 Ų buried · 27 hydrogen bonds · 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 P61586
- Every structure of UniProt Q9AJW7
- Elsewhere: RCSB PDB 3LXR · PDBe 3LXR · UniProt P61586 · UniProt Q9AJW7
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