Research workbench
OXYR2 E204G variant (cl-bound) from vibrio vulnificus
Analyse OXYR2 E204G variant (cl-bound) from vibrio vulnificus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5X0Q
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysr family transcriptional regulator
- UniProt
- A0A087I947
- Ligands
- CL
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lysr family transcriptional regulator | protein | 212 | 33% helix, 26% strand | A0A087I947 |
Ligands and binding sites
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 | 260 | 0.48 | 0.73 | 31 | empty |
| 2 | 263 | 0.48 | 0.73 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 308 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5X0Q · OxyR2 E204G variant (Cl-bound) from Vibrio vulnificus · 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 A0A087I947
- Elsewhere: RCSB PDB 5X0Q · PDBe 5X0Q · UniProt A0A087I947
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