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Yorodumi- PDB-1v49: Solution structure of microtubule-associated protein light chain-3 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v49 | ||||||
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Title | Solution structure of microtubule-associated protein light chain-3 | ||||||
Components | Microtubule-associated proteins 1A/1B light chain 3B | ||||||
Keywords | STRUCTURAL PROTEIN / UBIQUITIN FOLD | ||||||
Function / homology | Function and homology information SARS-CoV-2 modulates autophagy / ceramide binding / autophagy of mitochondrion / cellular response to nitrogen starvation / phosphatidylethanolamine binding / Translation of Replicase and Assembly of the Replication Transcription Complex / TBC/RABGAPs / Macroautophagy / Receptor Mediated Mitophagy / axoneme ...SARS-CoV-2 modulates autophagy / ceramide binding / autophagy of mitochondrion / cellular response to nitrogen starvation / phosphatidylethanolamine binding / Translation of Replicase and Assembly of the Replication Transcription Complex / TBC/RABGAPs / Macroautophagy / Receptor Mediated Mitophagy / axoneme / autophagosome maturation / autophagosome membrane / mitophagy / organelle membrane / autophagosome assembly / autophagosome / endomembrane system / PINK1-PRKN Mediated Mitophagy / Pexophagy / cellular response to starvation / mitochondrial membrane / macroautophagy / autophagy / KEAP1-NFE2L2 pathway / Translation of Replicase and Assembly of the Replication Transcription Complex / cytoplasmic vesicle / microtubule binding / microtubule / intracellular membrane-bounded organelle / ubiquitin protein ligase binding / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Kouno, T. / Mizuguchi, M. / Tanida, I. / Ueno, T. / Kominami, E. / Kawano, K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Solution structure of microtubule-associated protein light chain 3 and identification of its functional subdomains. Authors: Kouno, T. / Mizuguchi, M. / Tanida, I. / Ueno, T. / Kanematsu, T. / Mori, Y. / Shinoda, H. / Hirata, M. / Kominami, E. / Kawano, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1v49.cif.gz | 53.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v49.ent.gz | 40.1 KB | Display | PDB format |
PDBx/mmJSON format | 1v49.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v4/1v49 ftp://data.pdbj.org/pub/pdb/validation_reports/v4/1v49 | 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 | Mass: 14150.283 Da / Num. of mol.: 1 / Fragment: residues 1-120 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX-6P / Production host: Escherichia coli (E. coli) / References: UniProt: Q9GZQ8 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 230 / pH: 7.0 / Pressure: 1 atm / 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 AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |