Research workbench
AlphaFold monomer V2.0 prediction for CRISPR-associated protein CSE2 (Q53VY0)
Analyse AlphaFold monomer V2.0 prediction for CRISPR-associated protein CSE2 (Q53VY0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q53VY0
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF336F3B74E376B91b0149E66DCdF03429c696250
- UniProt
- Q53VY0
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 169 | — | Q53VY0 |
Compared structures
- 2ZCA · Crystal structure of TTHB189, a CRISPR-associated protein, CSE2 family from thermus… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 2ZCA · Crystal Structure of TTHB189, a CRISPR-associated protein, Cse2 family from Thermus… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 4H7A · Crystal structure of CasB from Thermus thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 4H7A · Crystal structure of casb from thermus thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.91
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 Q53VY0
- Elsewhere: UniProt Q53VY0 · AlphaFold DB Q53VY0
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