Research workbench
Crystal structure of rhogdi LYS(135,138,141)TYR mutant
Analyse Crystal structure of rhogdi LYS(135,138,141)TYR mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BXW
- Type
- protein
- Length
- 276 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho GDP-dissociation inhibitor 1
- UniProt
- P52565
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Rho GDP-dissociation inhibitor 1 | protein | 138 | 6% helix, 57% strand | P52565 |
Ligands and binding sites
- FMT · Formic acid · additive · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.53 | 0.83 | 20 | empty |
| 2 | 88 | 0.51 | 0.83 | 21 | TRS |
Interfaces
1 interface between chains.
- A–B · 676 Ų buried · 5 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 P52565
- Elsewhere: RCSB PDB 2BXW · PDBe 2BXW · UniProt P52565
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.