Research workbench
Epsilon subunit and ATP complex of F1F0-ATP synthase from the Thermophilic Bacillus PS3
Analyse Epsilon subunit and ATP complex of F1F0-ATP synthase from the Thermophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E5Y
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.92
- Source
- Bacillus sp. PS3
- Molecule
- ATP synthase epsilon chain
- EC
- 3.6.3.14
- UniProt
- P07678
- Ligands
- ATP
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · resolution 1.92 · 1 distinct chain · 27% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP synthase epsilon chain (EC 3.6.3.14) | protein | 133 | 27% helix, 48% strand | P07678 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 701 | 0.71 | 0.78 | 62 | ATP |
| 2 | 57 | 0.27 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1050 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2E5Y · Epsilon subunit and ATP complex of F1F0-ATP synthase from the thermophilic bacillus PS3 · the same entry in another collection · chain A against A, TM-score 1.00
- P07678 · AlphaFold monomer V2.0 prediction for ATP synthase epsilon chain (P07678) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P07678
- Elsewhere: RCSB PDB 2E5Y · PDBe 2E5Y · UniProt P07678
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