Research workbench
Ligand binding domain of the wild-type aspartate receptor with aspartate
Analyse Ligand binding domain of the wild-type aspartate receptor with aspartate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VLT
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate receptor
- UniProt
- P02941
- Ligands
- ASP
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate receptor | protein | 142 | 78% helix, 0% strand | P02941 |
| B | Aspartate receptor | protein | 143 | 73% helix, 0% strand | P02941 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 751 | 0.70 | 0.77 | 63 | empty |
| 2 | 51 | 0.40 | 0.82 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1002 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1VLT · Ligand binding domain of the wild-type aspartate receptor with aspartate · the same entry in another collection · chain A against A, TM-score 1.00
- P02941 · AlphaFold monomer V2.0 prediction for methyl-accepting chemotaxis protein II (P02941) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P02941
- Elsewhere: RCSB PDB 1VLT · PDBe 1VLT · UniProt P02941
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