Research workbench
AlphaFold monomer V2.0 prediction for elongation factor P--(R)-beta- lysine ligase (C5BDL9)
Analyse AlphaFold monomer V2.0 prediction for elongation factor P--(R)-beta- lysine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5BDL9
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6b3373535645884b693Bc933E91A27320E504095
- UniProt
- C5BDL9
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 325 | — | C5BDL9 |
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 C5BDL9
- Elsewhere: UniProt C5BDL9 · AlphaFold DB C5BDL9
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