Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP1A (P18203)
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
- P18203
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- UniProt
- P18203
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 108 | — | P18203 |
Compared structures
- 1FKK · Atomic structure of FKBP12, an immunophilin binding protein · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1FKK · Atomic structure of FKBP12, an immunophilin binding protein · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1FKL · Atomic structure of FKBP12-rapaymycin, an immunophilin-immunosuppressant complex · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 1FKL · Atomic structure of FKBP12-rapaymycin, an immunophilin- immunosuppressant complex · an experimental structure of the same protein · chain A against A, TM-score 0.97
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 P18203
- Elsewhere: UniProt P18203 · AlphaFold DB P18203
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.