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Yorodumi- PDB-1b4q: Solution structure of human thioltransferase complex with glutathione -
+Open data
-Basic information
Entry | Database: PDB / ID: 1b4q | ||||||
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Title | Solution structure of human thioltransferase complex with glutathione | ||||||
Components | PROTEIN (HUMAN THIOLTRANSFERASE) | ||||||
Keywords | OXIDOREDUCTASE / HUMAN THIOLTRANSFERASE / DISULFIDE INTERMEDIATE / GLUTATHIONE | ||||||
Function / homology | Function and homology information glutathione disulfide oxidoreductase activity / positive regulation of membrane potential / nucleobase-containing small molecule interconversion / Interconversion of nucleotide di- and triphosphates / sodium channel regulator activity / extracellular exosome / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Yang, Y. / Jao, S.C. / Nanduri, S. / Starke, D.W. / Mieyal, J.J. / Qin, J. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Authors: Yang, Y. / Jao, S. / Nanduri, S. / Starke, D.W. / Mieyal, J.J. / Qin, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b4q.cif.gz | 735.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b4q.ent.gz | 632.9 KB | Display | PDB format |
PDBx/mmJSON format | 1b4q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b4/1b4q ftp://data.pdbj.org/pub/pdb/validation_reports/b4/1b4q | 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: 11592.254 Da / Num. of mol.: 1 / Mutation: C7S, C25S, C78S, C82S Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH GLUTATHIONE / Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P35754 |
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#2: Chemical | ChemComp-GSH / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED HUMAN THIOLTRANSFERASE MUTANT (C7S,C25S,C78S,C82S). THE STRUCTURE CALCULATION IS BASED ON A TOTAL OF ...Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED HUMAN THIOLTRANSFERASE MUTANT (C7S,C25S,C78S,C82S). THE STRUCTURE CALCULATION IS BASED ON A TOTAL OF 2658 EXPERIMENTAL CONSTRAINTS |
-Sample preparation
Sample conditions | pH: 6.0 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian VARIAN INOVA 500 / Manufacturer: Varian / Model: VARIAN INOVA 500 / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformers calculated total number: 95 / Conformers submitted total number: 21 |