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The crystal structure of R60E mutant of the histidine kinase (kinb) sensor domain from pseudomonas aeruginosa PA01
Analyse The crystal structure of R60E mutant of the histidine kinase (kinb) sensor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LLC
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable two-component sensor
- UniProt
- Q9HT87
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable two-component sensor | protein | 124 | 78% helix, 0% strand | Q9HT87 |
| B | Probable two-component sensor | protein | 120 | 80% helix, 0% strand | Q9HT87 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.73 | 0.84 | 37 | TRS |
| 2 | 72 | 0.59 | 0.89 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1040 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4LLC · The crystal structure of R60E mutant of the histidine kinase (KinB) sensor domain from… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9HT87
- Elsewhere: RCSB PDB 4LLC · PDBe 4LLC · UniProt Q9HT87
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