Research workbench
Structure of the B. subtilis RNA polymerase in complex with held (dimer)
Analyse Structure of the B. subtilis RNA polymerase in complex with held (dimer) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZFB
- Type
- protein
- Length
- 7,313 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-directed RNA polymerase subunit delta; RNA polymerase subunit omega; DNA-directed RNA…
- EC
- 2.7.7.6, 3.6.4.12
- UniProt
- A0A410WI33, A0A063XB83, A0A2J0WBQ0, A0A063XB23, A0A164TSE8
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 8 distinct chains · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, d | DNA-directed RNA polymerase subunit delta | protein | 139 | 58% helix, 4% strand | — |
| E, e | RNA polymerase subunit omega | protein | 69 | 23% helix, 28% strand | A0A410WI33 |
| U, u | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 231 | 26% helix, 27% strand | A0A063XB83 |
| V, v | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 227 | 23% helix, 21% strand | A0A063XB83 |
| X | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1093 | 26% helix, 24% strand | A0A2J0WBQ0 |
| Y, y | DNA-directed RNA polymerase subunit beta' (EC 2.7.7.6) | protein | 1127 | 41% helix, 10% strand | A0A063XB23 |
| H, h | DNA helicase (EC 3.6.4.12) | protein | 771 | 49% helix, 8% strand | A0A164TSE8 |
| x | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1092 | 25% helix, 23% strand | A0A2J0WBQ0 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains Y, y
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.83 | 0.85 | 94 | empty |
| 2 | 1028 | 0.82 | 0.83 | 101 | empty |
| 3 | 678 | 0.81 | 0.85 | 92 | empty |
| 4 | 1064 | 0.81 | 0.82 | 105 | empty |
| 5 | 1135 | 0.81 | 0.82 | 101 | empty |
Interfaces
34 interfaces between chains.
- x–y · 5689 Ų buried · 42 hydrogen bonds · protein-protein
- X–Y · 5623 Ų buried · 40 hydrogen bonds · protein-protein
- y–h · 4523 Ų buried · 32 hydrogen bonds · protein-protein
- Y–H · 4484 Ų buried · 30 hydrogen bonds · protein-protein
- u–v · 2026 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6ZFB · Structure of the B. subtilis RNA POLYMERASE in complex with HelD (dimer) · the same entry in another collection · chain D against D, 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 A0A410WI33
- Every structure of UniProt A0A063XB83
- Every structure of UniProt A0A2J0WBQ0
- Every structure of UniProt A0A063XB23
- Every structure of UniProt A0A164TSE8
- Elsewhere: RCSB PDB 6ZFB · PDBe 6ZFB · UniProt A0A410WI33 · UniProt A0A063XB83 · UniProt A0A2J0WBQ0 · UniProt A0A063XB23 · UniProt A0A164TSE8
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