Research workbench
Crystal structure of anti-anti-sigma factor phyr I40V/S51C mutant from bartonella quintana
Analyse Crystal structure of anti-anti-sigma factor phyr I40V/S51C mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UXV
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensory transduction regulatory protein
- UniProt
- A0A0H3LUV4
- Pockets
- 4 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensory transduction regulatory protein | protein | 244 | 60% helix, 11% strand | A0A0H3LUV4 |
| B | Sensory transduction regulatory protein | protein | 240 | 61% helix, 11% strand | A0A0H3LUV4 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.43 | 0.75 | 23 | empty |
| 2 | 129 | 0.38 | 0.73 | 20 | empty |
| 3 | 68 | 0.31 | 0.75 | 20 | empty |
| 4 | 67 | 0.29 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 377 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5UXV · Crystal Structure of Anti-anti-sigma factor PhyR I40V/S51C mutant from Bartonella quintana · 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 A0A0H3LUV4
- Elsewhere: RCSB PDB 5UXV · PDBe 5UXV · UniProt A0A0H3LUV4
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