Research workbench
AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase (P50098)
Analyse AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P50098
- Type
- protein
- Length
- 512 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa178cE677748B9f80A2a9921a7edc5C39EDB037A
- UniProt
- P50098
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 512 | — | P50098 |
Compared structures
- 8C51 · Trypanosoma brucei IMP dehydrogenase (cyto) crystallized in High Five cells revealing… · an experimental structure of the same protein · chain A against A, TM-score 0.76
- 8C53 · Trypanosoma brucei IMP dehydrogenase (ori) crystallized in High Five cells reveals native… · an experimental structure of the same protein · chain A against A, TM-score 0.76
- 8CGY · Trypanosoma brucei IMP dehydrogenase (ori) crystallized in High Five cells reveals native… · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 6RFU · In cellulo crystallization of trypanosoma brucei imp dehydrogenase enables the… · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 6RFU · In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the… · an experimental structure of the same protein · chain A against B, TM-score 0.76
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 P50098
- Elsewhere: UniProt P50098 · AlphaFold DB P50098
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.