Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C (B5EFG1)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5EFG1
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- NADH-quinone oxidoreductase subunit C
- UniProt
- B5EFG1
Structure
1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C | protein | 161 | 27% helix, 30% strand | B5EFG1 |
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 B5EFG1
- Elsewhere: UniProt B5EFG1 · AlphaFold DB B5EFG1
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