Research workbench
Crystal structure of the ligand binding domain of the bacterial serine chemoreceptor tsr
Analyse Crystal structure of the ligand binding domain of the bacterial serine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D4U
- Type
- protein
- Length
- 322 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein I
- UniProt
- P02942
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein I | protein | 167 | 85% helix, 0% strand | P02942 |
| B | Methyl-accepting chemotaxis protein I | protein | 155 | 85% helix, 0% strand | P02942 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.63 | 0.84 | 22 | empty |
| 2 | 206 | 0.62 | 0.82 | 21 | empty |
| 3 | 255 | 0.57 | 0.78 | 33 | empty |
| 4 | 229 | 0.48 | 0.75 | 33 | empty |
| 5 | 86 | 0.34 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1830 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2D4U · Crystal Structure of the ligand binding domain of the bacterial serine chemoreceptor Tsr · 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 0.97
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 P02942
- Elsewhere: RCSB PDB 2D4U · PDBe 2D4U · UniProt P02942
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