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Crystal structure of rsbq
Analyse Crystal structure of rsbq in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WOM
- Type
- protein
- Length
- 541 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sigma factor sigb regulation protein rsbq
- UniProt
- O07015
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sigma factor sigb regulation protein rsbq | protein | 271 | 49% helix, 18% strand | O07015 |
| B | Sigma factor sigb regulation protein rsbq | protein | 270 | 49% helix, 19% strand | O07015 |
Ligands and binding sites
- PGO · S-1,2-propanediol · additive · 12 copies · chains A, B
- MLA · Malonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 910 | 0.79 | 0.81 | 81 | PGO |
| 2 | 91 | 0.35 | 0.75 | 21 | empty |
| 3 | 64 | 0.33 | 0.76 | 20 | PGO |
Interfaces
1 interface between chains.
- A–B · 692 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 O07015
- Elsewhere: RCSB PDB 1WOM · PDBe 1WOM · UniProt O07015
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