Research workbench
Ligand binding domain of pseudomonas aeruginosa PAO1 amino acid chemoreceptors pctb in complex with L-gln
Analyse Ligand binding domain of pseudomonas aeruginosa PAO1 amino acid chemoreceptors… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LTO
- Type
- protein
- Length
- 479 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein pctb
- UniProt
- A0A0F6UK01
- Ligands
- GLN, SO4
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein pctb | protein | 237 | 33% helix, 27% strand | A0A0F6UK01 |
| B | Methyl-accepting chemotaxis protein pctb | protein | 242 | 35% helix, 25% strand | A0A0F6UK01 |
Ligands and binding sites
- GLN · Glutamine · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.35 | 0.76 | 13 | empty |
| 2 | 52 | 0.30 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 709 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5LTO · Ligand binding domain of Pseudomonas aeruginosa PAO1 amino acid chemoreceptors PctB in… · the same entry in another collection · chain B against B, 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 A0A0F6UK01
- Elsewhere: RCSB PDB 5LTO · PDBe 5LTO · UniProt A0A0F6UK01
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