Research workbench
Co-crystal structure of the sigma factor rpoe in complex with the anti-sigma factor nepr from bartonella quintana
Analyse Co-crystal structure of the sigma factor rpoe in complex with the anti-sigma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UXX
- Type
- protein
- Length
- 417 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase sigma factor; Anti-sigma factor nepr
- UniProt
- A0A0H3M3R8, A0A0H3LV19
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase sigma factor | protein | 160 | 68% helix, 0% strand | A0A0H3M3R8 |
| B | Anti-sigma factor nepr | protein | 46 | 65% helix, 0% strand | A0A0H3LV19 |
| C | RNA polymerase sigma factor | protein | 163 | 70% helix, 0% strand | A0A0H3M3R8 |
| D | Anti-sigma factor nepr | protein | 48 | 63% helix, 0% strand | A0A0H3LV19 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.86 | 0.94 | 56 | empty |
| 2 | 89 | 0.48 | 0.82 | 19 | empty |
| 3 | 120 | 0.45 | 0.78 | 20 | empty |
| 4 | 107 | 0.43 | 0.78 | 17 | empty |
| 5 | 94 | 0.41 | 0.77 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1984 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1856 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 896 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 813 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 391 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 5UXX · Co-crystal structure of the sigma factor RpoE in complex with the anti-sigma factor NepR… · 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 A0A0H3M3R8
- Every structure of UniProt A0A0H3LV19
- Elsewhere: RCSB PDB 5UXX · PDBe 5UXX · UniProt A0A0H3M3R8 · UniProt A0A0H3LV19
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