Research workbench
AlphaFold monomer V2.0 prediction for isocitrate dehydrogenase [NADP] (P50216)
Analyse AlphaFold monomer V2.0 prediction for isocitrate dehydrogenase [NADP] (P50216) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P50216
- Type
- protein
- Length
- 738 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
- UniProt
- P50216
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 738 | — | P50216 |
Compared structures
- 3MBC · Crystal structure of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 3MBC · Crystal structure of monomeric isocitrate dehydrogenase from corynebacterium glutamicum… · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 2B0T · Structure of monomeric NADP isocitrate dehydrogenase · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 2B0T · Structure of Monomeric NADP Isocitrate dehydrogenase · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 P50216
- Elsewhere: UniProt P50216 · AlphaFold DB P50216
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