+Open data
-Basic information
Entry | Database: PDB / ID: 2op7 | ||||||
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Title | WW4 | ||||||
Components | NEDD4-like E3 ubiquitin-protein ligase WWP1 | ||||||
Keywords | LIGASE / WW domain / Beta sheet | ||||||
Function / homology | Function and homology information HECT-type E3 ubiquitin transferase / ubiquitin ligase complex / Downregulation of ERBB4 signaling / monoatomic ion transmembrane transport / central nervous system development / Stimuli-sensing channels / ubiquitin-protein transferase activity / Regulation of RUNX2 expression and activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation ...HECT-type E3 ubiquitin transferase / ubiquitin ligase complex / Downregulation of ERBB4 signaling / monoatomic ion transmembrane transport / central nervous system development / Stimuli-sensing channels / ubiquitin-protein transferase activity / Regulation of RUNX2 expression and activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / proteasome-mediated ubiquitin-dependent protein catabolic process / protein ubiquitination / symbiont entry into host cell / negative regulation of DNA-templated transcription / signal transduction / extracellular exosome / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Qin, H.N. / Li, M.F. / Pu, H. / Sankaran, S. / Ahmed, S. / Song, J.X. | ||||||
Citation | Journal: To be Published Title: NMR structure of the forth WW domain of WWP1 Authors: Qin, H.N. / Li, M.F. / Pu, H. / Sankaran, S. / Ahmed, S. / Song, J.X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2op7.cif.gz | 122.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2op7.ent.gz | 98.4 KB | Display | PDB format |
PDBx/mmJSON format | 2op7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/op/2op7 ftp://data.pdbj.org/pub/pdb/validation_reports/op/2op7 | HTTPS FTP |
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-Related structure data
Similar structure data |
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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/peptide | Mass: 4705.121 Da / Num. of mol.: 1 / Fragment: residues 494-532 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: WWP1 / Plasmid: PGEX4T1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 References: UniProt: Q9H0M0, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.3 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker INOVA / Manufacturer: Bruker / Model: INOVA / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 1000 / Conformers submitted total number: 10 |