Research workbench
The crystal structure of lobe domain of E. COLI RNA polymerase complexed with the C-terminal domain of uvrd
Analyse The crystal structure of lobe domain of E. COLI RNA polymerase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EGS
- Type
- protein
- Length
- 348 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-directed RNA polymerase subunit beta; DNA helicase II
- EC
- 2.7.7.6, 3.6.4.12
- UniProt
- P0A8V2, P03018
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 293 | 33% helix, 23% strand | P0A8V2 |
| B | DNA helicase II (EC 3.6.4.12) | protein | 55 | 11% helix, 51% strand | P03018 |
Ligands and binding sites
- GOL · Glycerol · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.58 | 0.80 | 30 | empty |
| 2 | 248 | 0.58 | 0.79 | 34 | empty |
| 3 | 97 | 0.42 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 555 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7EGS · The crystal structure of lobe domain of E. coli RNA polymerase complexed with the… · the same entry in another collection · chain A against A, TM-score 1.00
- P03018 · AlphaFold monomer V2.0 prediction for DNA helicase II (P03018) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P0A8V2
- Every structure of UniProt P03018
- Elsewhere: RCSB PDB 7EGS · PDBe 7EGS · UniProt P0A8V2 · UniProt P03018
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