Research workbench
Structure of the ligand binding domain of the bacterial serine chemoreceptor tsr with ligand
Analyse Structure of the ligand binding domain of the bacterial serine chemoreceptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ATP
- Type
- protein
- Length
- 302 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein I
- UniProt
- P02942
- Ligands
- SER
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein I | protein | 151 | 80% helix, 0% strand | P02942 |
| B | Methyl-accepting chemotaxis protein I | protein | 151 | 81% helix, 0% strand | P02942 |
Ligands and binding sites
- SER · Serine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 763 | 0.73 | 0.79 | 69 | empty |
Interfaces
1 interface between chains.
- A–B · 1499 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 3ATP · Structure of the ligand binding domain of the bacterial serine chemoreceptor Tsr with… · the same entry in another collection · chain A against A, TM-score 1.00
- P02942 · AlphaFold monomer V2.0 prediction for methyl-accepting chemotaxis protein I (P02942) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P02942
- Elsewhere: RCSB PDB 3ATP · PDBe 3ATP · UniProt P02942
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