Research workbench
AlphaFold monomer V2.0 prediction for energy-coupling factor transporter ATP-binding protein ECFA1 (Q1J449)
Analyse AlphaFold monomer V2.0 prediction for energy-coupling factor transporter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1J449
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x00f48420072d220CAe17e7bEf8eCf4C6dbFcAcfF
- Molecule
- Energy-coupling factor transporter ATP-binding protein ECFA1
- UniProt
- Q1J449
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Energy-coupling factor transporter ATP-binding protein ECFA1 | protein | 279 | 42% helix, 21% strand | Q1J449 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.64 | 0.80 | 23 | empty |
| 2 | 54 | 0.41 | 0.81 | 13 | empty |
| 3 | 85 | 0.34 | 0.74 | 17 | empty |
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 Q1J449
- Elsewhere: UniProt Q1J449 · AlphaFold DB Q1J449
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