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- PDB-2nbv: Solution structure of the Rpn13 Pru domain engaging the hPLIC2 UB... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2nbv | ||||||
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Title | Solution structure of the Rpn13 Pru domain engaging the hPLIC2 UBL domain | ||||||
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![]() | PROTEIN BINDING | ||||||
Function / homology | ![]() negative regulation of G protein-coupled receptor internalization / negative regulation of clathrin-dependent endocytosis / positive regulation of ERAD pathway / regulation of autophagosome assembly / proteasome regulatory particle, lid subcomplex / molecular function inhibitor activity / proteasome binding / endopeptidase activator activity / autophagosome assembly / autophagosome ...negative regulation of G protein-coupled receptor internalization / negative regulation of clathrin-dependent endocytosis / positive regulation of ERAD pathway / regulation of autophagosome assembly / proteasome regulatory particle, lid subcomplex / molecular function inhibitor activity / proteasome binding / endopeptidase activator activity / autophagosome assembly / autophagosome / polyubiquitin modification-dependent protein binding / proteasome assembly / regulation of macroautophagy / ERAD pathway / proteasome complex / molecular condensate scaffold activity / transcription elongation by RNA polymerase II / UCH proteinases / Cargo recognition for clathrin-mediated endocytosis / cytoplasmic vesicle / ubiquitin-dependent protein catabolic process / protease binding / proteasome-mediated ubiquitin-dependent protein catabolic process / Ub-specific processing proteases / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Chen, X. / Walters, K.J. | ||||||
![]() | ![]() Title: Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome. Authors: Chen, X. / Randles, L. / Shi, K. / Tarasov, S.G. / Aihara, H. / Walters, K.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2nbuC ![]() 2nbwC ![]() 5irsC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 16742.045 Da / Num. of mol.: 1 / Fragment: residues 1-150 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 8764.189 Da / Num. of mol.: 1 / Fragment: residues 26-103 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The starting structures are PDB enries 1J8C and 5IRS. | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |