Research workbench
AlphaFold monomer V2.0 prediction for chloramphenicol acetyltransferase (P26841)
Analyse AlphaFold monomer V2.0 prediction for chloramphenicol acetyltransferase (P26841) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26841
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x59a703CF5f3d296F946D2f7C100865462A66F361
- UniProt
- P26841
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 212 | — | P26841 |
Compared structures
- 2XAT · Complex of the hexapeptide xenobiotic acetyltransferase with chloramphenicol and… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 2XAT · Complex of the hexapeptide xenobiotic acetyltransferase with chloramphenicol and… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1XAT · Structure of the hexapeptide xenobiotic acetyltransferase from pseudomonas aeruginosa · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1XAT · Structure of the hexapeptide xenobiotic acetyltransferase from pseudomonas aeruginosa · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 P26841
- Elsewhere: UniProt P26841 · AlphaFold DB P26841
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