+Open data
-Basic information
Entry | Database: PDB / ID: 2ai6 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of human phosphohistidine phosphatase 1 | ||||||
Components | 14 kDa phosphohistidine phosphatase | ||||||
Keywords | HYDROLASE / alpha/beta architecture | ||||||
Function / homology | Function and homology information phosphohistidine phosphatase / peptidyl-histidine dephosphorylation / negative regulation of lyase activity / negative regulation of ATP citrate synthase activity / protein histidine phosphatase activity / lamellipodium organization / leading edge of lamellipodium / positive regulation of cell motility / negative regulation of T cell receptor signaling pathway / calcium channel inhibitor activity ...phosphohistidine phosphatase / peptidyl-histidine dephosphorylation / negative regulation of lyase activity / negative regulation of ATP citrate synthase activity / protein histidine phosphatase activity / lamellipodium organization / leading edge of lamellipodium / positive regulation of cell motility / negative regulation of T cell receptor signaling pathway / calcium channel inhibitor activity / protein dephosphorylation / actin filament binding / actin cytoskeleton organization / transmembrane transporter binding / nuclear body / extracellular exosome / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Authors | Gong, W. / Cui, G. / Jin, C. / Xia, B. | ||||||
Citation | Journal: Biochem.J. / Year: 2009 Title: Solution structure and catalytic mechanism of human protein histidine phosphatase 1. Authors: Gong, W. / Li, Y. / Cui, G. / Hu, J. / Fang, H. / Jin, C. / Xia, B. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2ai6.cif.gz | 777.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2ai6.ent.gz | 658 KB | Display | PDB format |
PDBx/mmJSON format | 2ai6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ai/2ai6 ftp://data.pdbj.org/pub/pdb/validation_reports/ai/2ai6 | HTTPS FTP |
---|
-Related structure data
Related structure data | 2ozxC C: citing same article (ref.) |
---|---|
Similar structure data | |
Other databases |
|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 13851.521 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET28A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21DE3 References: UniProt: Q9NRX4, Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1mM PHPT1, 50mM PBS, 50mM NaCl, 30mM DTT; 90%H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | pH: 7.2 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 Details: torsion angle dynamics performed by DYANA, simulated annealing performed by AMBER | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 100 / Conformers submitted total number: 21 |