Download MendeleyMBP-fusion protein of myosin-binding protein c residues 149-269
Rebowski, G., Boczkowska, M., Dominguez, R.To be published.
4EDQ | pdb_00004edq
MBP-fusion protein of myosin-binding protein c residues 149-269
- PDB DOI: https://doi.org/10.2210/pdb4EDQ/pdb
- Classification: TRANSPORT PROTEIN/CONTRACTILE PROTEIN
- Organism(s): Escherichia coli K-12, Mus musculus
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2012-03-27 Released: 2013-03-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.64 ?
- R-Value Free: 0.214 (Depositor), 0.220 (DCC)
- R-Value Work: 0.172 (Depositor), 0.170 (DCC)
- R-Value Observed: 0.173 (Depositor)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 2.1 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 |
| Maltose-binding periplasmic protein,Myosin-binding protein C, cardiac-type chimeric protein | 492 | Escherichia coli K-12, Mus musculus This entity is chimeric | Mutation(s): 0 Gene Names: malE, b4034, JW3994 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O70468 (Mus musculus) Explore O70468 Go to UniProtKB: O70468 | |||||
IMPC: MGI:102844 | |||||
Find proteins for P0AEX9 (Escherichia coli (strain K12)) Explore P0AEX9 Go to UniProtKB: P0AEX9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Groups | P0AEX9O70468 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Oligosaccharides
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
| PRD_900009 Query on PRD_900009 | C, D | alpha-maltotriose | Oligosaccharide / Nutrient |  | |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.64 ?
- R-Value Free: 0.214 (Depositor), 0.220 (DCC)
- R-Value Work: 0.172 (Depositor), 0.170 (DCC)
- R-Value Observed: 0.173 (Depositor)
Space Group: P 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 53.993 | ¦Á = 85.73 |
| b = 60.7 | ¦Â = 79.2 |
| c = 73.314 | ¦Ă = 89.98 |
| Software Name | Purpose |
|---|---|
| JDirector | data collection |
| PHENIX | model building |
| PHENIX | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
| PHENIX | phasing |
Entry History
Deposition Data
- Released Date: 2013-03-20 Deposition Author(s): Rebowski, G., Boczkowska, M., Dominguez, R.
Revision History (Full details and data files)
- Version 1.0: 2013-03-20
Type: Initial release - Version 1.1: 2017-07-26
Changes: Data collection, Source and taxonomy - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Structure summary - Version 2.1: 2023-09-13
Changes: Data collection, Database references, Refinement description, Structure summary
