Research workbench
Crystal structure of the nitrate transporter NRT1.1 from arabidopsis thaliana in complex with nitrate.
Analyse Crystal structure of the nitrate transporter NRT1.1 from arabidopsis thaliana… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A2O
- Type
- protein
- Length
- 940 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrate transporter 1.1
- UniProt
- Q05085
- Ligands
- NO3
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nitrate transporter 1.1 | protein | 470 | 70% helix, 0% strand | Q05085 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1009 | 0.80 | 0.81 | 78 | NO3 |
| 2 | 966 | 0.80 | 0.81 | 80 | NO3 |
| 3 | 346 | 0.73 | 0.84 | 27 | empty |
| 4 | 567 | 0.68 | 0.78 | 64 | empty |
| 5 | 105 | 0.43 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1096 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5A2O · Crystal structure of the nitrate transporter NRT1.1 from Arabidopsis thaliana in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- Q05085 · AlphaFold monomer V2.0 prediction for protein NRT1/ ptr family 6.3 (Q05085) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q05085
- Elsewhere: RCSB PDB 5A2O · PDBe 5A2O · UniProt Q05085
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