Research workbench
Crystal structure of putative transcriptional regulator lysr from vibrio parahaemolyticus
Analyse Crystal structure of putative transcriptional regulator lysr from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QSX
- Type
- protein
- Length
- 365 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative transcriptional regulator, lysr family
- UniProt
- Q87RY9
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative transcriptional regulator, lysr family | protein | 180 | 31% helix, 33% strand | Q87RY9 |
| B | Putative transcriptional regulator, lysr family | protein | 185 | 36% helix, 31% strand | Q87RY9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.79 | 0.99 | 18 | empty |
| 2 | 96 | 0.53 | 0.83 | 15 | SO4 |
| 3 | 109 | 0.52 | 0.82 | 20 | SO4 |
| 4 | 52 | 0.30 | 0.77 | 13 | empty |
| 5 | 55 | 0.28 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1380 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2QSX · Crystal structure of putative transcriptional regulator LysR From Vibrio parahaemolyticus · 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 Q87RY9
- Elsewhere: RCSB PDB 2QSX · PDBe 2QSX · UniProt Q87RY9
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