Research workbench
Cryoem structure of E.COLI his pause elongation complex
Analyse Cryoem structure of E.COLI his pause elongation complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ASX
- Type
- protein + DNA + RNA
- Length
- 3,252 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (32-mer); RNA (29-mer); DNA-directed RNA polymerase subunit alpha; DNA-directed RNA…
- EC
- 2.7.7.6
- UniProt
- P0A7Z4, P0A8V2, P0A8T7, P0A800
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 8 distinct chains · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA (32-mer) | dna | 22 | — | — |
| B | DNA (32-mer) | dna | 30 | — | — |
| R | RNA (29-mer) | rna | 21 | — | — |
| G | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 220 | 21% helix, 35% strand | P0A7Z4 |
| H | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 220 | 15% helix, 37% strand | P0A7Z4 |
| I | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1318 | 29% helix, 20% strand | P0A8V2 |
| J | DNA-directed RNA polymerase subunit beta' (EC 2.7.7.6) | protein | 1338 | 35% helix, 16% strand | P0A8T7 |
| K | DNA-directed RNA polymerase subunit omega (EC 2.7.7.6) | protein | 83 | 66% helix, 0% strand | P0A800 |
Ligands and binding sites
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 | 1103 | 0.84 | 0.85 | 103 | empty |
| 2 | 841 | 0.83 | 0.86 | 68 | empty |
| 3 | 772 | 0.82 | 0.85 | 73 | empty |
| 4 | 1071 | 0.80 | 0.81 | 82 | empty |
| 5 | 942 | 0.78 | 0.80 | 89 | empty |
Interfaces
15 interfaces between chains.
- I–J · 8611 Ų buried · 87 hydrogen bonds · protein-protein
- G–I · 1812 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 1792 Ų buried · 9 hydrogen bonds · protein-protein
- J–K · 1289 Ų buried · 11 hydrogen bonds · protein-protein
- B–J · 1117 Ų buried · 13 hydrogen bonds · protein-nucleic
Compared structures
- 6ASX · CryoEM structure of E.coli his pause elongation complex · the same entry in another collection · chain K against K, TM-score 1.00
- P0A8V2 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta (P0A8V2) · a predicted model of the same protein · chain I against A, TM-score 0.97
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 P0A7Z4
- Every structure of UniProt P0A8V2
- Every structure of UniProt P0A8T7
- Every structure of UniProt P0A800
- Elsewhere: RCSB PDB 6ASX · PDBe 6ASX · UniProt P0A7Z4 · UniProt P0A8V2 · UniProt P0A8T7 · UniProt P0A800
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