Research workbench
AlphaFold monomer V2.0 prediction for pyrroline-5-carboxylate reductase 3 (Q4R531)
Analyse AlphaFold monomer V2.0 prediction for pyrroline-5-carboxylate reductase 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4R531
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6227512B0B04f05c48A3f9Bb2A26C737dAb650E8
- Molecule
- Pyrroline-5-carboxylate reductase 3
- UniProt
- Q4R531
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 58% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyrroline-5-carboxylate reductase 3 | protein | 274 | 58% helix, 14% strand | Q4R531 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 533 | 0.59 | 0.73 | 47 | empty |
| 2 | 75 | 0.42 | 0.80 | 21 | empty |
| 3 | 139 | 0.41 | 0.75 | 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 Q4R531
- Elsewhere: UniProt Q4R531 · AlphaFold DB Q4R531
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