Research workbench
AlphaFold monomer V2.0 prediction for elongation factor P--(R)-beta- lysine ligase (B5FRL4)
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
- B5FRL4
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- UniProt
- B5FRL4
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 325 | — | B5FRL4 |
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 B5FRL4
- Elsewhere: UniProt B5FRL4 · AlphaFold DB B5FRL4
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