+Open data
-Basic information
Entry | Database: PDB / ID: 2mp0 | ||||||
---|---|---|---|---|---|---|---|
Title | Protein Phosphorylation upon a Fleeting Encounter | ||||||
Components |
| ||||||
Keywords | TRANSFERASE / EIN EIIAGlc complex | ||||||
Function / homology | Function and homology information negative regulation of carbohydrate metabolic process / phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / phosphoenolpyruvate-dependent sugar phosphotransferase system / transmembrane transporter complex / kinase activity / identical protein binding ...negative regulation of carbohydrate metabolic process / phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / phosphoenolpyruvate-dependent sugar phosphotransferase system / transmembrane transporter complex / kinase activity / identical protein binding / membrane / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | fewest violations, model1 | ||||||
Authors | Xing, Q. / Yang, J. / Huang, P. / Zhang, W. / Tang, C. | ||||||
Citation | Journal: Angew.Chem.Int.Ed.Engl. / Year: 2014 Title: Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling. Authors: Xing, Q. / Huang, P. / Yang, J. / Sun, J.Q. / Gong, Z. / Dong, X. / Guo, D.C. / Chen, S.M. / Yang, Y.H. / Wang, Y. / Yang, M.H. / Yi, M. / Ding, Y.M. / Liu, M.L. / Zhang, W.P. / Tang, C. #1: Journal: Angew.Chem.Int.Ed.Engl. / Year: 2014 Title: Visualizing an Ultra-Weak Protein-Protein Interaction in Phosphorylation Signaling Authors: Xing, Q. / Huang, P. / Yang, J. / Sun, J. / Gong, Z. / Dong, X. / Guo, D. / Chen, S. / Yang, Y. / Wang, Y. / Yang, M. / Yi, M. / Ding, Y. / Liu, M. / Zhang, W. / Tang, C. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2mp0.cif.gz | 135.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2mp0.ent.gz | 105.6 KB | Display | PDB format |
PDBx/mmJSON format | 2mp0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mp0_validation.pdf.gz | 424.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2mp0_full_validation.pdf.gz | 432.6 KB | Display | |
Data in XML | 2mp0_validation.xml.gz | 12.9 KB | Display | |
Data in CIF | 2mp0_validation.cif.gz | 17.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/2mp0 ftp://data.pdbj.org/pub/pdb/validation_reports/mp/2mp0 | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 28224.121 Da / Num. of mol.: 1 / Fragment: N-terminal Domain, residues 1-258 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: ptsI / Production host: Escherichia coli (E. coli) / Strain (production host): G1698 References: UniProt: P08839, phosphoenolpyruvate-protein phosphotransferase |
---|---|
#2: Protein | Mass: 18141.834 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: crr / Production host: Escherichia coli (E. coli) References: UniProt: P69783, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor |
#3: Chemical | ChemComp-PO3 / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||||||||||||||||||||||||
Sample conditions | pH: 7.4 / Temperature: 313.4 K |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 90 / Conformers submitted total number: 1 / Representative conformer: 1 |