Research workbench
Crystal structure of thermus aquaticus RNA polymerase sigma subunit fragment containing regions 1.2 to 3.1
Analyse Crystal structure of thermus aquaticus RNA polymerase sigma subunit fragment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KU2
- Type
- protein
- Length
- 480 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sigma factor siga
- UniProt
- Q9EZJ8
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sigma factor siga | protein | 240 | 69% helix, 0% strand | Q9EZJ8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.77 | 0.98 | 20 | empty |
| 2 | 212 | 0.60 | 0.81 | 26 | empty |
| 3 | 165 | 0.49 | 0.77 | 20 | empty |
| 4 | 120 | 0.41 | 0.75 | 21 | empty |
| 5 | 90 | 0.35 | 0.75 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 2237 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 1KU2 · Crystal Structure of Thermus aquaticus RNA Polymerase Sigma Subunit Fragment Containing… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9EZJ8 · AlphaFold monomer V2.0 prediction for RNA polymerase sigma factor siga (Q9EZJ8) · a predicted model of the same protein · chain A against A, TM-score 0.67
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 Q9EZJ8
- Elsewhere: RCSB PDB 1KU2 · PDBe 1KU2 · UniProt Q9EZJ8
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