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AlphaFold monomer V2.0 prediction for protein NRT1/ ptr family 2.3 (Q9M175)
Analyse AlphaFold monomer V2.0 prediction for protein NRT1/ ptr family 2.3 (Q9M175) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9M175
- Type
- protein
- Length
- 558 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3e0aC98Dc58EA794394EdeA1992f0D3Ca753d03c
- Molecule
- Protein NRT1/ ptr family 2.3
- UniProt
- Q9M175
- Pockets
- 4 · best druggability 0.81
Structure
1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein NRT1/ ptr family 2.3 | protein | 558 | 70% helix, 1% strand | Q9M175 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1041 | 0.81 | 0.82 | 79 | empty |
| 2 | 222 | 0.48 | 0.74 | 20 | empty |
| 3 | 130 | 0.42 | 0.74 | 17 | empty |
| 4 | 57 | 0.30 | 0.75 | 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 Q9M175
- Elsewhere: UniProt Q9M175 · AlphaFold DB Q9M175
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