Research workbench
AlphaFold monomer V2.0 prediction for 1-pyrroline-5-carboxylate dehydrogenase (P99076)
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
- P99076
- Type
- protein
- Length
- 514 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- 1-pyrroline-5-carboxylate dehydrogenase
- UniProt
- P99076
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-pyrroline-5-carboxylate dehydrogenase | protein | 514 | 41% helix, 22% strand | P99076 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.67 | 0.83 | 44 | empty |
| 2 | 362 | 0.64 | 0.79 | 37 | empty |
| 3 | 57 | 0.50 | 0.86 | 15 | empty |
| 4 | 54 | 0.28 | 0.75 | 16 | 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 P99076
- Elsewhere: UniProt P99076 · AlphaFold DB P99076
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