Research workbench
AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P24750)
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
- P24750
- Type
- protein
- Length
- 294 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
- Molecule
- Glyceraldehyde-3-phosphate dehydrogenase
- UniProt
- P24750
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glyceraldehyde-3-phosphate dehydrogenase | protein | 294 | 28% helix, 27% strand | P24750 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.69 | 0.79 | 42 | empty |
| 2 | 319 | 0.64 | 0.80 | 36 | empty |
| 3 | 72 | 0.35 | 0.77 | 19 | empty |
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 P24750
- Elsewhere: UniProt P24750 · AlphaFold DB P24750
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