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Structure of the P. aeruginosa LasR ligand-binding domain bound to its autoinducer
Analyse Structure of the P. aeruginosa LasR ligand-binding domain bound to its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UV0
- Type
- protein
- Length
- 660 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- PSEUDOMONAS AERUGINOSA
- Molecule
- Transcriptional activator protein lasr
- UniProt
- P25084
- Ligands
- OHN
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · resolution 1.8 · 4 distinct chains · 55% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Transcriptional activator protein lasr | protein | 163 | 56% helix, 17% strand | P25084 |
| F | Transcriptional activator protein lasr | protein | 164 | 54% helix, 16% strand | P25084 |
| G | Transcriptional activator protein lasr | protein | 166 | 55% helix, 17% strand | P25084 |
| H | Transcriptional activator protein lasr | protein | 167 | 56% helix, 17% strand | P25084 |
Ligands and binding sites
- OHN · N-3-oxo-dodecanoyl-L-homoserine lactone · ligand · 4 copies · chains E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.81 | 0.97 | 28 | OHN |
| 2 | 146 | 0.81 | 0.97 | 28 | OHN |
| 3 | 142 | 0.81 | 0.97 | 28 | OHN |
| 4 | 142 | 0.80 | 0.97 | 29 | OHN |
| 5 | 277 | 0.57 | 0.77 | 35 | empty |
Interfaces
4 interfaces between chains.
- E–G · 966 Ų buried · 15 hydrogen bonds · protein-protein
- F–H · 927 Ų buried · 12 hydrogen bonds · protein-protein
- F–G · 371 Ų buried · 1 hydrogen bond · protein-protein
- E–H · 192 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2UV0 · Structure of the P. aeruginosa lasr ligand-binding domain bound to its autoinducer · the same entry in another collection · chain H against H, TM-score 1.00
- P25084 · AlphaFold monomer V2.0 prediction for transcriptional activator protein lasr (P25084) · a predicted model of the same protein · chain F against A, TM-score 0.98
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 P25084
- Elsewhere: RCSB PDB 2UV0 · PDBe 2UV0 · UniProt P25084
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