Research workbench
Crystal structure of a heterotrimeric G-protein subunit from entamoeba histolytica, ehg-alpha-1
Analyse Crystal structure of a heterotrimeric G-protein subunit from entamoeba… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FID
- Type
- protein
- Length
- 622 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- G protein alpha subunit
- UniProt
- C4M483
- Ligands
- GDP
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | G protein alpha subunit | protein | 318 | 47% helix, 14% strand | C4M483 |
| B | G protein alpha subunit | protein | 304 | 44% helix, 14% strand | C4M483 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 526 | 0.78 | 0.86 | 72 | GDP |
| 2 | 215 | 0.70 | 0.87 | 29 | empty |
| 3 | 319 | 0.68 | 0.83 | 46 | GDP |
| 4 | 142 | 0.48 | 0.78 | 19 | empty |
| 5 | 55 | 0.42 | 0.82 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1005 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 26 modified (engineered, methylation).
Compared structures
- 4FID · Crystal structure of a heterotrimeric G-Protein subunit from entamoeba histolytica… · 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 C4M483
- Elsewhere: RCSB PDB 4FID · PDBe 4FID · UniProt C4M483
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.