Research workbench
AlphaFold monomer V2.0 prediction for probable peptidoglycan endopeptidase lyte (P54421)
Analyse AlphaFold monomer V2.0 prediction for probable peptidoglycan endopeptidase lyte… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P54421
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC993df6B6Eb50E5885B4dbc9C1205fD18d103dA4
- UniProt
- P54421
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 334 | — | P54421 |
Compared structures
- 8I2F · Crystal structure of Bacillus subtilis LytE catalytic domain in complex with IseA · an experimental structure of the same protein · chain A against B, TM-score 0.35
- 8I2E · Crystal structure of Bacillus subtilis LytE in complex with IseA · an experimental structure of the same protein · chain A against B, TM-score 0.35
- 8I2D · Crystal structure of Bacillus subtilis LytE · an experimental structure of the same protein · chain A against A, TM-score 0.35
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 P54421
- Elsewhere: UniProt P54421 · AlphaFold DB P54421
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