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Yorodumi- PDB-1k8o: Solution Structure of the Lipoic Acid-Bearing Domain of the E2 co... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1k8o | ||||||
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Title | Solution Structure of the Lipoic Acid-Bearing Domain of the E2 component of Human, Mitochondrial Branched-Chain alpha-Ketoacid Dehydrogenase | ||||||
Components | E2 component of Branched-Chain alpha-Ketoacid Dehydrogenase | ||||||
Keywords | TRANSFERASE / Lipoyl Acid Bearing / Human BCKD / Experimental NMR data | ||||||
Function / homology | Function and homology information dihydrolipoyllysine-residue (2-methylpropanoyl)transferase / dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity / : / lipoic acid binding / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / Glyoxylate metabolism and glycine degradation / mitochondrial nucleoid / acetyltransferase activity / RHOH GTPase cycle ...dihydrolipoyllysine-residue (2-methylpropanoyl)transferase / dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity / : / lipoic acid binding / branched-chain amino acid catabolic process / Branched-chain amino acid catabolism / Glyoxylate metabolism and glycine degradation / mitochondrial nucleoid / acetyltransferase activity / RHOH GTPase cycle / microtubule cytoskeleton / mitochondrial matrix / ubiquitin protein ligase binding / mitochondrion / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing, molecular dynamics torsion angle dynamics | ||||||
Authors | Chang, C.-F. / Chou, H.-T. / Chuang, J.L. / Chuang, D.T. / Huang, T.-h. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex Authors: Chang, C.-F. / Chou, H.-T. / Chuang, J.L. / Chuang, D.T. / Huang, T.-h. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1k8o.cif.gz | 590 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1k8o.ent.gz | 505.9 KB | Display | PDB format |
PDBx/mmJSON format | 1k8o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k8/1k8o ftp://data.pdbj.org/pub/pdb/validation_reports/k8/1k8o | HTTPS FTP |
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-Related structure data
Related structure data | 1k8mC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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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: 10662.938 Da / Num. of mol.: 1 / Fragment: LIPOIC ACID-BEARING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET28b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 References: UniProt: P11182, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups |
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-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 |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing, molecular dynamics torsion angle dynamics Software ordinal: 1 | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structure with the lowest energy and acceptable covalent geometry Conformers calculated total number: 100 / Conformers submitted total number: 20 |