Research workbench
Crystal structure of Burkholderia thailandensis MftR in complex with uric acid
Analyse Crystal structure of Burkholderia thailandensis MftR in complex with uric acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8YLK
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Burkholderia thailandensis
- Molecule
- MarR family transcriptional regulator
- UniProt
- A0A2N8QSC4
- Ligands
- URC
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 67% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MarR family transcriptional regulator | protein | 153 | 67% helix, 7% strand | A0A2N8QSC4 |
Ligands and binding sites
- URC · Uric acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 245 | 0.49 | 0.74 | 30 | URC |
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 A0A2N8QSC4
- Elsewhere: RCSB PDB 8YLK · PDBe 8YLK · UniProt A0A2N8QSC4
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