Research workbench
The closed ring structure of the rho transcription termination factor in complex with nucleic acid in the motor domains
Analyse The closed ring structure of the rho transcription termination factor in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HT1
- Type
- protein + RNA
- Length
- 657 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AG30
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| J, K | — | rna | 2 | — | — |
| M | — | rna | 5 | — | — |
| A, B | — | protein | 324 | — | P0AG30 |
Compared structures
- 2HT1 · The closed ring structure of the Rho transcription termination factor in complex with… · the same entry in another collection · chain M against M, TM-score 1.00
- P0AG30 · AlphaFold monomer V2.0 prediction for transcription termination factor rho (P0AG30) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P0AG30
- Elsewhere: RCSB PDB 2HT1 · PDBe 2HT1 · UniProt P0AG30
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