+Open data
-Basic information
Entry | Database: PDB / ID: 2mul | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of the UBM1 domain of human HUWE1/ARF-BP1 | ||||||
Components | E3 ubiquitin-protein ligase HUWE1 | ||||||
Keywords | PROTEIN BINDING / Ubiquitin Binding Motif | ||||||
Function / homology | Function and homology information negative regulation of mitochondrial fusion / histone ubiquitin ligase activity / positive regulation of mitophagy in response to mitochondrial depolarization / HECT-type E3 ubiquitin transferase / positive regulation of protein targeting to mitochondrion / Golgi organization / protein monoubiquitination / positive regulation of protein ubiquitination / base-excision repair / circadian regulation of gene expression ...negative regulation of mitochondrial fusion / histone ubiquitin ligase activity / positive regulation of mitophagy in response to mitochondrial depolarization / HECT-type E3 ubiquitin transferase / positive regulation of protein targeting to mitochondrion / Golgi organization / protein monoubiquitination / positive regulation of protein ubiquitination / base-excision repair / circadian regulation of gene expression / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / secretory granule lumen / ficolin-1-rich granule lumen / membrane fusion / cell differentiation / Golgi membrane / Neutrophil degranulation / mitochondrion / DNA binding / RNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Authors | Farhadi, S. / Khatun, R. / Lemak, A. / Kaustov, L. / Ramabadran, R. / Hunter, H. / Sheng, Y. | ||||||
Citation | Journal: To be Published Title: Solution structure of Ubiquitin Binding Motif of human Arf-bp1 Authors: Khatun, R. / Sheng, Y. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2mul.cif.gz | 305.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2mul.ent.gz | 265.6 KB | Display | PDB format |
PDBx/mmJSON format | 2mul.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/2mul ftp://data.pdbj.org/pub/pdb/validation_reports/mu/2mul | HTTPS FTP |
---|
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 5663.181 Da / Num. of mol.: 1 / Fragment: UNP residues 2951-3003 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX2TK / Production host: Escherichia coli (E. coli) / References: UniProt: Q7Z6Z7 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 0.4 mM [U-13C; U-15N] protein, 300 mM sodium chloride, 2.7 mM potassium chloride, 10 mM sodium phosphate, 2 mM potassium phosphate, 0.05 mM CHAPS, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||||||||||
Sample conditions | Ionic strength: 300 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 700 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |