Research workbench
Structure of H. salinarum rosr (VNG0258) grown from kbr
Analyse Structure of H. salinarum rosr (VNG0258) grown from kbr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FAQ
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA binding protein
- UniProt
- Q9HSF4
- Ligands
- BR, SO4
- Pockets
- 1 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA binding protein | protein | 110 | 67% helix, 13% strand | Q9HSF4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.83 | 0.97 | 29 | BR |
Interfaces
1 interface between chains.
- A–B · 2055 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6FAQ · Structure of H. salinarum RosR (vng0258) grown from KBr · 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 Q9HSF4
- Elsewhere: RCSB PDB 6FAQ · PDBe 6FAQ · UniProt Q9HSF4
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