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Yorodumi- PDB-2bdo: SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A... -
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-Basic information
Entry | Database: PDB / ID: 2bdo | ||||||
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Title | SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY | ||||||
Components | PROTEIN (ACETYL-COA CARBOXYLASE) | ||||||
Keywords | BIOTIN / BIOTINYL DOMAIN / ACETYL COA CARBOXYLASE / SWINGING ARM / NMR SPECTROSCOPY / PROTEIN STRUCTURE | ||||||
Function / homology | Function and homology information acetyl-CoA carboxylase complex / malonyl-CoA biosynthetic process / acetyl-CoA carboxylase activity / fatty acid biosynthetic process / molecular adaptor activity / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Roberts, E.L. / Shu, N. / Howard, M.J. / Broadhurst, R.W. / Chapman-Smith, A. / Wallace, J.C. / Morris, T. / Cronan, J.E. / Perham, R.N. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Authors: Roberts, E.L. / Shu, N. / Howard, M.J. / Broadhurst, R.W. / Chapman-Smith, A. / Wallace, J.C. / Morris, T. / Cronan Jr., J.E. / Perham, R.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bdo.cif.gz | 560 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bdo.ent.gz | 465.3 KB | Display | PDB format |
PDBx/mmJSON format | 2bdo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2bdo_validation.pdf.gz | 377.1 KB | Display | wwPDB validaton report |
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Full document | 2bdo_full_validation.pdf.gz | 603.3 KB | Display | |
Data in XML | 2bdo_validation.xml.gz | 54.1 KB | Display | |
Data in CIF | 2bdo_validation.cif.gz | 78.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bd/2bdo ftp://data.pdbj.org/pub/pdb/validation_reports/bd/2bdo | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8700.017 Da / Num. of mol.: 1 / Fragment: BIOTINYL DOMAIN, RESIDUES 77 - 156 Source method: isolated from a genetically manipulated source Details: BIOTINYL DOMAIN MADE BY EXPRESSING BIOTIN DOMAIN SUBGENE IN A STRAIN IN WHICH BIOTIN PROTEIN LIGASE IS ALSO EXPRESSED, LEADING TO PARTIAL BIOTINYLATION IN VIVO Source: (gene. exp.) Escherichia coli (E. coli) / Strain: BL21(DE3) / Plasmid: PTM53 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0ABD8, acetyl-CoA carboxylase |
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#2: Chemical | ChemComp-BTN / |
-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 PROTEIN |
-Sample preparation
Sample conditions | Ionic strength: 20mM SODIUM PHOSPHATE / pH: 6.8 / Pressure: 1 atm / Temperature: 303 K |
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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 | Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 40 / Conformers submitted total number: 23 |