Research workbench
AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P00361)
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
- P00361
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE14c7d3573074F3F9DC243BEDa64BaBcFD04DeA7
- UniProt
- P00361
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 331 | — | P00361 |
Compared structures
- 1CER · Determinants of enzyme thermostability observed in the molecular structure of thermus… · an experimental structure of the same protein · chain A against O, TM-score 0.99
- 1CER · Determinants of enzyme thermostability observed in the molecular structure of thermus… · an experimental structure of the same protein · chain A against O, TM-score 0.99
- 2G82 · High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase… · an experimental structure of the same protein · chain A against O, TM-score 0.99
- 2G82 · High resolution structures of thermus aquaticus glyceraldehyde-3- phosphate… · an experimental structure of the same protein · chain A against O, 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 P00361
- Elsewhere: UniProt P00361 · AlphaFold DB P00361
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