Research workbench
AlphaFold monomer V2.0 prediction for glycerol-1-phosphate dehydrogenase [NAD(P)+] (A3MTM6)
Analyse AlphaFold monomer V2.0 prediction for glycerol-1-phosphate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3MTM6
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8e3a917A16E8163577aA515EA010E513A6d710df
- UniProt
- A3MTM6
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 338 | — | A3MTM6 |
Compared structures
- 5FB3 · Structure of glycerophosphate dehydrogenase in complex with NADPH · an experimental structure of the same protein · chain A against F, TM-score 0.99
- 5FB3 · Structure of glycerophosphate dehydrogenase in complex with NADPH · an experimental structure of the same protein · chain A against F, 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 A3MTM6
- Elsewhere: UniProt A3MTM6 · AlphaFold DB A3MTM6
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