Research workbench
AlphaFold monomer V2.0 prediction for NAD(P) transhydrogenase subunit beta (P0C188)
Analyse AlphaFold monomer V2.0 prediction for NAD(P) transhydrogenase subunit beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0C188
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA81476e932072E01982403F6C56fd30fc8575e48
- Molecule
- NAD(P) transhydrogenase subunit beta
- UniProt
- P0C188
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 63% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P) transhydrogenase subunit beta | protein | 464 | 63% helix, 8% strand | P0C188 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.72 | 0.86 | 40 | empty |
| 2 | 780 | 0.66 | 0.74 | 70 | empty |
| 3 | 121 | 0.41 | 0.75 | 23 | empty |
| 4 | 87 | 0.41 | 0.78 | 15 | empty |
| 5 | 61 | 0.32 | 0.76 | 19 | empty |
Compared structures
- 2OO5 · Structure of transhydrogenase (dI.H2NADH)2(dIII.NADP+)1 asymmetric complex · an experimental structure of the same protein · chain A against C, TM-score 0.37
- 2OO5 · Structure of transhydrogenase (DI.H2NADH)2(DIII.NADP+)1 asymmetric complex · an experimental structure of the same protein · chain A against C, TM-score 0.37
- 2OOR · Structure of transhydrogenase (dI.NAD+)2(dIII.H2NADPH)1 asymmetric complex · an experimental structure of the same protein · chain A against C, TM-score 0.37
- 2OOR · Structure of transhydrogenase (DI.NAD+)2(DIII.H2NADPH)1 asymmetric complex · an experimental structure of the same protein · chain A against C, TM-score 0.37
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 P0C188
- Elsewhere: UniProt P0C188 · AlphaFold DB P0C188
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