Research workbench
AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P00355)
Analyse AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P00355
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- UniProt
- P00355
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 333 | — | P00355 |
Compared structures
- 5TSO · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pig muscle complexed… · an experimental structure of the same protein · chain A against P, TM-score 1.00
- 5TSO · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pig muscle complexed… · an experimental structure of the same protein · chain A against P, TM-score 1.00
- 5DDI · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pig muscle - holo… · an experimental structure of the same protein · chain A against P, TM-score 0.98
- 5DDI · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pig muscle - holo… · an experimental structure of the same protein · chain A against P, TM-score 0.98
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 P00355
- Elsewhere: UniProt P00355 · AlphaFold DB P00355
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