Download Mendeleystructural basis of transcription elongation control: the NusA-aCTD complex
Prasch, S., Schweimer, K., Roesch, P.To be published.
2JZB
Solution structure of the complex between E.coli NusA-AR2 and RNAP-aCTD
- PDB DOI: https://doi.org/10.2210/pdb2JZB/pdb
- BMRB: 15614
- Classification: TRANSFERASE/transcription
- Organism(s): Yersinia pseudotuberculosis, Escherichia coli
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-01-02 Released: 2009-04-28
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 240
- Conformers Submitted: 20
- Selection Criteria: structures with the lowest energy
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| DNA-directed RNA polymerase subunit alpha | 99 | Yersinia pseudotuberculosis | Mutation(s): 0 Gene Names: rpoA EC: 2.7.7.6 |  | |
UniProt | |||||
Find proteins for Q664U6 (Yersinia pseudotuberculosis serotype I (strain IP32953)) Explore Q664U6 Go to UniProtKB: Q664U6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q664U6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Transcription elongation protein nusA | 74 | Escherichia coli | Mutation(s): 0 Gene Names: nusA |  | |
UniProt | |||||
Find proteins for P0AFF6 (Escherichia coli (strain K12)) Explore P0AFF6 Go to UniProtKB: P0AFF6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0AFF6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 240
- Conformers Submitted: 20
- Selection Criteria: structures with the lowest energy
Entry History
Deposition Data
- Released Date: 2009-04-28 Deposition Author(s): Prasch, S., Schweimer, K., Roesch, P.
Revision History (Full details and data files)
- Version 1.0: 2009-04-28
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2020-02-19
Changes: Data collection, Database references, Derived calculations, Other
