Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic (Q9SCY2)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9SCY2
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x29F5a997C9c963C0f8d9eA83ae506aA675743654
- UniProt
- Q9SCY2
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 208 | — | Q9SCY2 |
Compared structures
- 1Y0O · crystal structure of reduced AtFKBP13 · an experimental structure of the same protein · chain A against D, TM-score 0.60
- 1Y0O · Crystal structure of reduced ATFKBP13 · an experimental structure of the same protein · chain A against D, TM-score 0.60
- 1U79 · Crystal structure of ATFKBP13 · an experimental structure of the same protein · chain A against D, TM-score 0.60
- 1U79 · Crystal structure of AtFKBP13 · an experimental structure of the same protein · chain A against D, TM-score 0.60
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 Q9SCY2
- Elsewhere: UniProt Q9SCY2 · AlphaFold DB Q9SCY2
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