Research workbench
Crystal structure of the E. COLI transcription termination factor rho
Analyse Crystal structure of the E. COLI transcription termination factor rho in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7X2R
- Type
- protein
- Length
- 2,457 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription termination factor rho
- EC
- 3.6.4.-
- UniProt
- A0A377BS88
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Transcription termination factor rho (EC 3.6.4.-) | protein | 408 | 41% helix, 21% strand | A0A377BS88 |
| B | Transcription termination factor rho (EC 3.6.4.-) | protein | 411 | 40% helix, 16% strand | A0A377BS88 |
| D | Transcription termination factor rho (EC 3.6.4.-) | protein | 409 | 41% helix, 20% strand | A0A377BS88 |
| F | Transcription termination factor rho (EC 3.6.4.-) | protein | 413 | 38% helix, 14% strand | A0A377BS88 |
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1100 | 0.81 | 0.82 | 96 | empty |
| 2 | 891 | 0.80 | 0.82 | 85 | empty |
| 3 | 1128 | 0.79 | 0.81 | 111 | empty |
| 4 | 665 | 0.78 | 0.84 | 70 | empty |
| 5 | 887 | 0.77 | 0.80 | 60 | empty |
Interfaces
6 interfaces between chains.
- C–E · 1395 Ų buried · 12 hydrogen bonds · protein-protein
- D–F · 1383 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 1318 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1158 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1158 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7X2R · Crystal structure of the E. coli transcription termination factor Rho · the same entry in another collection · chain A against A, 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 A0A377BS88
- Elsewhere: RCSB PDB 7X2R · PDBe 7X2R · UniProt A0A377BS88
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