Research workbench
AlphaFold monomer V2.0 prediction for sodium-dependent proline transporter (P28573)
Analyse AlphaFold monomer V2.0 prediction for sodium-dependent proline transporter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28573
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Sodium-dependent proline transporter
- UniProt
- P28573
- Pockets
- 6 · best druggability 0.81
Structure
1 distinct chain · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sodium-dependent proline transporter | protein | 637 | 69% helix, 2% strand | P28573 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.81 | 0.82 | 85 | empty |
| 2 | 893 | 0.73 | 0.77 | 79 | empty |
| 3 | 90 | 0.60 | 0.88 | 16 | empty |
| 4 | 64 | 0.37 | 0.79 | 19 | empty |
| 5 | 55 | 0.34 | 0.76 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P28573
- Elsewhere: UniProt P28573 · AlphaFold DB P28573
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