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Crystal structure of a widely conserved GTPase era
Analyse Crystal structure of a widely conserved GTPase era in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EGA
- Type
- protein
- Length
- 585 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (GTP-binding protein era)
- UniProt
- P06616
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (GTP-binding protein era) | protein | 292 | 36% helix, 24% strand | P06616 |
| B | Protein (GTP-binding protein era) | protein | 293 | 36% helix, 24% strand | P06616 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 709 | 0.73 | 0.79 | 70 | SO4 |
| 2 | 769 | 0.72 | 0.78 | 64 | SO4 |
| 3 | 117 | 0.38 | 0.75 | 26 | empty |
| 4 | 82 | 0.32 | 0.73 | 17 | empty |
| 5 | 78 | 0.31 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 771 Ų buried · 17 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 P06616
- Elsewhere: RCSB PDB 1EGA · PDBe 1EGA · UniProt P06616
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