Research workbench
Cryoem structure of E.COLI RNA polymerase elongation complex bound to nusg (the consensus nusg-ec)
Analyse Cryoem structure of E.COLI RNA polymerase elongation complex bound to nusg (the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PY1
- Type
- protein + DNA + RNA
- Length
- 3,382 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ntdna; Tdna; RNA; DNA-directed RNA polymerase subunit alpha; DNA-directed RNA polymerase…
- EC
- 2.7.7.6
- UniProt
- P0A7Z4, P0A8V4, P0A8T8, P0A800, C3SID2
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 9 distinct chains · 30% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| N | Ntdna | dna | 30 | — | — |
| T | Tdna | dna | 34 | — | — |
| R | RNA | rna | 11 | — | — |
| A | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 221 | 19% helix, 34% strand | P0A7Z4 |
| B | DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6) | protein | 218 | 20% helix, 36% strand | P0A7Z4 |
| C | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1337 | 28% helix, 20% strand | P0A8V4 |
| D | DNA-directed RNA polymerase subunit beta' (EC 2.7.7.6) | protein | 1335 | 35% helix, 16% strand | P0A8T8 |
| E | DNA-directed RNA polymerase subunit omega (EC 2.7.7.6) | protein | 73 | 62% helix, 0% strand | P0A800 |
| G | Transcription TERMINATION/ANTITERMINATION protein nusg | protein | 123 | 28% helix, 15% strand | C3SID2 |
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 | 811 | 0.82 | 0.85 | 78 | empty |
| 2 | 1013 | 0.81 | 0.83 | 80 | empty |
| 3 | 587 | 0.80 | 0.86 | 65 | empty |
| 4 | 524 | 0.78 | 0.85 | 60 | empty |
| 5 | 788 | 0.78 | 0.81 | 77 | empty |
Interfaces
19 interfaces between chains.
- C–D · 8232 Ų buried · 60 hydrogen bonds · protein-protein
- A–B · 2025 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 1774 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 1229 Ų buried · 7 hydrogen bonds · protein-protein
- N–T · 1067 Ų buried · 68 hydrogen bonds · nucleic-nucleic
Compared structures
- 7PY1 · CryoEM structure of E.coli RNA polymerase elongation complex bound to NusG (the consensus… · the same entry in another collection · chain G against G, TM-score 1.00
- P0A8T8 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (P0A8T8) · a predicted model of the same protein · chain D against A, TM-score 0.92
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 P0A8V4
- Every structure of UniProt P0A8T8
- Every structure of UniProt P0A800
- Every structure of UniProt C3SID2
- Elsewhere: RCSB PDB 7PY1 · PDBe 7PY1 · UniProt P0A7Z4 · UniProt P0A8V4 · UniProt P0A8T8 · UniProt P0A800 · UniProt C3SID2
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