Research workbench
Ligand binding domain (lbd) of the P. aeruginosa histamine receptor tlpq
Analyse Ligand binding domain (lbd) of the P. aeruginosa histamine receptor tlpq in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FU4
- Type
- protein
- Length
- 1,174 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable chemotaxis transducer
- UniProt
- Q9I0I4
- Ligands
- HSM, PO4
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable chemotaxis transducer | protein | 297 | 40% helix, 29% strand | Q9I0I4 |
| B | Probable chemotaxis transducer | protein | 291 | 39% helix, 28% strand | Q9I0I4 |
| C | Probable chemotaxis transducer | protein | 296 | 41% helix, 29% strand | Q9I0I4 |
| D | Probable chemotaxis transducer | protein | 290 | 39% helix, 31% strand | Q9I0I4 |
Ligands and binding sites
- HSM · Histamine · ligand · 4 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 2 copies · chains A, C
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
- ACT · Acetate ion · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1003 | 0.73 | 0.76 | 112 | GOL |
| 2 | 152 | 0.63 | 0.85 | 36 | empty |
| 3 | 91 | 0.53 | 0.84 | 21 | empty |
| 4 | 317 | 0.52 | 0.73 | 56 | empty |
| 5 | 239 | 0.51 | 0.75 | 44 | empty |
Interfaces
5 interfaces between chains.
- A–B · 996 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 891 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 807 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 186 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 168 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 18 modified, 4 disulfide (engineered, disulfide).
Compared structures
- 6FU4 · Ligand binding domain (LBD) of the p. aeruginosa histamine receptor TlpQ · 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 Q9I0I4
- Elsewhere: RCSB PDB 6FU4 · PDBe 6FU4 · UniProt Q9I0I4
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