Research workbench
AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P17721)
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
- P17721
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1deF5d0757faedfe2A626225e579ACe5e2e425d2
- UniProt
- P17721
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 333 | — | P17721 |
Compared structures
- 1HDG · The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the… · an experimental structure of the same protein · chain A against Q, TM-score 0.99
- 1HDG · The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the… · an experimental structure of the same protein · chain A against Q, 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 P17721
- Elsewhere: UniProt P17721 · AlphaFold DB P17721
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