Research workbench
AlphaFold monomer V2.0 prediction for cbs domain-containing protein CBSX2, chloroplastic (Q9C5D0)
Analyse AlphaFold monomer V2.0 prediction for cbs domain-containing protein CBSX2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9C5D0
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3d6707a69900E10a2dEC242C7C8B483353cebf36
- UniProt
- Q9C5D0
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 238 | — | Q9C5D0 |
Compared structures
- 3SL7 · Crystal structure of CBS-pair protein, CBSX2 from Arabidopsis thaliana · an experimental structure of the same protein · chain A against A, TM-score 0.58
- 3SL7 · Crystal structure of cbs-pair protein, CBSX2 from arabidopsis thaliana · an experimental structure of the same protein · chain A against A, TM-score 0.58
- 4GQY · Crystal structure of CBSX2 in complex with AMP · an experimental structure of the same protein · chain A against C, TM-score 0.52
- 4GQY · Crystal structure of CBSX2 in complex with AMP · an experimental structure of the same protein · chain A against C, TM-score 0.52
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 Q9C5D0
- Elsewhere: UniProt Q9C5D0 · AlphaFold DB Q9C5D0
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