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Yorodumi- PDB-2n7k: Unveiling the structural determinants of KIAA0323 binding prefere... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2n7k | ||||||
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Title | Unveiling the structural determinants of KIAA0323 binding preference for NEDD8 | ||||||
Components |
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Keywords | SIGNALING PROTEIN | ||||||
Function / homology | Function and homology information regulation of proteolysis / protein neddylation / TGF-beta receptor signaling activates SMADs / anatomical structure morphogenesis / RNA endonuclease activity / Iron uptake and transport / protein modification process / cytoplasmic ribonucleoprotein granule / modification-dependent protein catabolic process / protein tag activity ...regulation of proteolysis / protein neddylation / TGF-beta receptor signaling activates SMADs / anatomical structure morphogenesis / RNA endonuclease activity / Iron uptake and transport / protein modification process / cytoplasmic ribonucleoprotein granule / modification-dependent protein catabolic process / protein tag activity / UCH proteinases / protein localization / Cargo recognition for clathrin-mediated endocytosis / Neddylation / ubiquitin-dependent protein catabolic process / mRNA binding / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / proteolysis / extracellular exosome / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Santonico, E. / Nepravishta, R. / Mattioni, A. / Valentini, E. / Mandaliti, W. / Procopio, R. / Iannuccelli, M. / Castagnoli, L. / Polo, S. / Paci, M. / Cesareni, G. | ||||||
Citation | Journal: To be Published Title: Unveiling the structural determinants of KIAA0323 binding preference for NEDD8 Authors: Santonico, E. / Nepravishta, R. / Mattioni, A. / Valentini, E. / Mandaliti, W. / Procopio, R. / Iannuccelli, M. / Castagnoli, L. / Polo, S. / Paci, M. / Cesareni, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n7k.cif.gz | 459.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n7k.ent.gz | 381.9 KB | Display | PDB format |
PDBx/mmJSON format | 2n7k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n7k_validation.pdf.gz | 415.3 KB | Display | wwPDB validaton report |
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Full document | 2n7k_full_validation.pdf.gz | 572.1 KB | Display | |
Data in XML | 2n7k_validation.xml.gz | 40.6 KB | Display | |
Data in CIF | 2n7k_validation.cif.gz | 52.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n7/2n7k ftp://data.pdbj.org/pub/pdb/validation_reports/n7/2n7k | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9086.562 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NEDD8 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15843 |
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#2: Protein | Mass: 6299.187 Da / Num. of mol.: 1 / Fragment: residues 627-678 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KHNYN, KIAA0323 / Production host: Escherichia coli (E. coli) / References: UniProt: O15037 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.15-1.5 mM [U-100% 15N] protein, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Units: mM / Component: entity_1-1 / Isotopic labeling: [U-100% 15N] / Conc. range: 0.15-1.5 |
Sample conditions | Ionic strength: 0.02 / pH: 5.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / 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: 11 |