Research workbench
AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P10096)
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
- P10096
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- UniProt
- P10096
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 333 | — | P10096 |
Compared structures
- 4O63 · Co-enzyme induced conformational changes in bovine eye glyceraldehyde 3-phosphate… · an experimental structure of the same protein · chain A against P, TM-score 0.99
- 4O63 · Co-enzyme Induced Conformational Changes in Bovine Eye Glyceraldehyde 3-Phosphate… · an experimental structure of the same protein · chain A against P, TM-score 0.99
- 4O59 · Co-enzyme Induced Conformational Changes in Bovine Eye Glyceraldehyde 3-Phosphate… · an experimental structure of the same protein · chain A against R, TM-score 0.99
- 4O59 · Co-enzyme induced conformational changes in bovine eye glyceraldehyde 3-phosphate… · an experimental structure of the same protein · chain A against R, TM-score 0.99
- 7U5M · Cryo-EM Structure of GAPDH · an experimental structure of the same protein · chain A against C, 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 P10096
- Elsewhere: UniProt P10096 · AlphaFold DB P10096
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