Research workbench
Ligand binding domain of pseudomonas aeruginosa PAO1 amino acid chemoreceptor pcta in complex with L-met
Analyse Ligand binding domain of pseudomonas aeruginosa PAO1 amino acid chemoreceptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LTX
- Type
- protein
- Length
- 478 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein
- UniProt
- A0A0H0Z019
- Ligands
- MET
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein | protein | 243 | 40% helix, 28% strand | A0A0H0Z019 |
| B | Chemotaxis protein | protein | 235 | 37% helix, 29% strand | A0A0H0Z019 |
Ligands and binding sites
- MET · Methionine · ligand · 2 copies · chains A, B
- FMT · Formic acid · additive · 6 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.58 | 0.76 | 25 | empty |
| 2 | 70 | 0.51 | 0.85 | 24 | MET |
| 3 | 114 | 0.38 | 0.75 | 28 | empty |
| 4 | 65 | 0.34 | 0.77 | 17 | GOL |
Interfaces
1 interface between chains.
- A–B · 1263 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 5LTX · Ligand binding domain of pseudomonas aeruginosa PAO1 amino acid chemoreceptor pcta in… · 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 A0A0H0Z019
- Elsewhere: RCSB PDB 5LTX · PDBe 5LTX · UniProt A0A0H0Z019
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