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Crystal structure of haemophilus influenzae luxs
Analyse Crystal structure of haemophilus influenzae luxs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J6W
- Type
- protein
- Length
- 321 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Autoinducer-2 production protein luxs
- UniProt
- P44007
- Ligands
- MET, ZN
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Autoinducer-2 production protein luxs | protein | 161 | 39% helix, 24% strand | P44007 |
| B | Autoinducer-2 production protein luxs | protein | 160 | 40% helix, 23% strand | P44007 |
Ligands and binding sites
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 | 183 | 0.75 | 0.91 | 32 | ZN, MET |
| 2 | 164 | 0.72 | 0.90 | 33 | ZN, MET |
| 3 | 59 | 0.30 | 0.75 | 15 | empty |
| 4 | 64 | 0.29 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2171 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
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 P44007
- Elsewhere: RCSB PDB 1J6W · PDBe 1J6W · UniProt P44007
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