Research workbench
AlphaFold monomer V2.0 prediction for F420-dependent NADP reductase (O29370)
Analyse AlphaFold monomer V2.0 prediction for F420-dependent NADP reductase (O29370) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O29370
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2aE8C900f2F869C24641aE78A9bb70D728467913
- UniProt
- O29370
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 212 | — | O29370 |
Compared structures
- 1JAX · Structure of coenzyme F420H2:NADP+ oxidoreductase (fno) · an experimental structure of the same protein · chain A against B, TM-score 1.00
- 1JAX · Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO) · an experimental structure of the same protein · chain A against B, TM-score 1.00
- 1JAY · Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO) with its substrates bound · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 1JAY · Structure of coenzyme F420H2:NADP+ oxidoreductase (fno) with its substrates bound · an experimental structure of the same protein · chain A against B, TM-score 0.99
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 O29370
- Elsewhere: UniProt O29370 · AlphaFold DB O29370
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