Research workbench
Cryoem structure of the transcription termination factor rho from mycobacterium tuberculosis
Analyse Cryoem structure of the transcription termination factor rho from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OQH
- Type
- protein
- Length
- 2,169 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A045J3H4
- Ligands
- ATP, MG
Structure
electron microscopy · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 363 | — | A0A045J3H4 |
| B | — | protein | 363 | — | A0A045J3H4 |
| C | — | protein | 361 | — | A0A045J3H4 |
| D | — | protein | 364 | — | A0A045J3H4 |
| E | — | protein | 362 | — | A0A045J3H4 |
| F | — | protein | 356 | — | A0A045J3H4 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 5 copies · chains B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OQH · CryoEM structure of the transcription termination factor Rho from Mycobacterium… · 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 A0A045J3H4
- Elsewhere: RCSB PDB 7OQH · PDBe 7OQH · UniProt A0A045J3H4
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