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Yorodumi- PDB-2ozw: Solution structure of human phosphohistidine phosphatase 1 with p... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ozw | ||||||
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Title | Solution structure of human phosphohistidine phosphatase 1 with phosphate ligand | ||||||
Components | 14 kDa phosphohistidine phosphatase | ||||||
Keywords | HYDROLASE / alpha/beta architecture / addition of phosphate ligand | ||||||
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 | ||||||
Model type details | minimized average | ||||||
Authors | Gong, W. / Cui, G. / Jin, C. / Xia, B. | ||||||
Citation | Journal: To be Published Title: Solution structure of phosphohistidine phosphatase 1 with phosphate ligand Authors: Gong, W. / Cui, G. / Jin, C. / Xia, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ozw.cif.gz | 778 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ozw.ent.gz | 653.8 KB | Display | PDB format |
PDBx/mmJSON format | 2ozw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ozw_validation.pdf.gz | 370.8 KB | Display | wwPDB validaton report |
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Full document | 2ozw_full_validation.pdf.gz | 497.4 KB | Display | |
Data in XML | 2ozw_validation.xml.gz | 35.8 KB | Display | |
Data in CIF | 2ozw_validation.cif.gz | 65 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oz/2ozw ftp://data.pdbj.org/pub/pdb/validation_reports/oz/2ozw | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-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 |
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#2: Chemical | ChemComp-PO4 / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1mM PHPT1, 50mM PBS, 50mM NaCl, 30mM DTT; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 7.2 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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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: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 100 / Conformers submitted total number: 21 |