Download MendeleyStructure of the complex between CbpA J-domain and CbpM provides a link between chaperone and transcription regulation in bacterial heat shock response
Sarraf, N.S., Shi, R., Zhang, L., Cygler, M., Ekiel, I.To be published.
3UCS
Crystal structure of the complex between CBPA J-domain and CBPM
- PDB DOI: https://doi.org/10.2210/pdb3UCS/pdb
- Classification: CHAPERONE
- Organism(s): Klebsiella pneumoniae 342, Escherichia coli K-12
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2011-10-27 Released: 2013-07-03
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.87 Å
- R-Value Free: 0.232
- R-Value Work: 0.196
- R-Value Observed: 0.198
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 |
| Chaperone-modulator protein CbpM | 102 | Klebsiella pneumoniae 342 | Mutation(s): 0 Gene Names: cbpM, KPK_5158 |  | |
UniProt | |||||
Find proteins for B5Y388 (Klebsiella pneumoniae (strain 342)) Explore B5Y388 Go to UniProtKB: B5Y388 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | B5Y388 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Curved DNA-binding protein | 74 | Escherichia coli K-12 | Mutation(s): 0 Gene Names: b1000, cbpA, JW0985 |  | |
UniProt | |||||
Find proteins for P36659 (Escherichia coli (strain K12)) Explore P36659 Go to UniProtKB: P36659 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P36659 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.87 Å
- R-Value Free: 0.232
- R-Value Work: 0.196
- R-Value Observed: 0.198
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 52.816 | α = 90 |
| b = 77.094 | β = 90 |
| c = 111.231 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| HKL-2000 | data reduction |
| SHARP | phasing |
Entry History
Deposition Data
- Released Date: 2013-07-03 Deposition Author(s): Shi, R., Sarraf, N.S., Cygler, M., Ekiel, I., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
Revision History (Full details and data files)
- Version 1.0: 2013-07-03
Type: Initial release - Version 1.1: 2017-11-08
Changes: Refinement description - Version 1.2: 2024-02-28
Changes: Data collection, Database references
