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AlphaFold monomer V2.0 prediction for 1-pyrroline-5-carboxylate dehydrogenase (A8F9T1)
Analyse AlphaFold monomer V2.0 prediction for 1-pyrroline-5-carboxylate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8F9T1
- Type
- protein
- Length
- 515 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x82Ec1Bda42ddFecD6D4b6f0a9d55b51b2c260362
- Molecule
- 1-pyrroline-5-carboxylate dehydrogenase
- UniProt
- A8F9T1
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-pyrroline-5-carboxylate dehydrogenase | protein | 515 | 41% helix, 23% strand | A8F9T1 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.71 | 0.86 | 43 | empty |
| 2 | 299 | 0.59 | 0.78 | 36 | 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 A8F9T1
- Elsewhere: UniProt A8F9T1 · AlphaFold DB A8F9T1
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