[English] 日本語
Yorodumi- PDB-1bdo: STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bdo | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING | ||||||
Components | ACETYL-COA CARBOXYLASE | ||||||
Keywords | TRANSFERASE / BCCPSC / CARBOXYL TRANSFERASE / FATTY ACID BIOSYNTHESIS / HAMMERHEAD STRUCTURE / SELENOMETHIONINE / LIGASE | ||||||
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 | X-RAY DIFFRACTION / SYNCHROTRON / A MODIFIED MAD PROCEDURE. SOFTWARE USED : NULL STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL / Resolution: 1.8 Å | ||||||
Authors | Athappilly, F.K. / Hendrickson, W.A. | ||||||
Citation | Journal: Structure / Year: 1995 Title: Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Authors: Athappilly, F.K. / Hendrickson, W.A. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1bdo.cif.gz | 29.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1bdo.ent.gz | 18.8 KB | Display | PDB format |
PDBx/mmJSON format | 1bdo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bdo_validation.pdf.gz | 417.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1bdo_full_validation.pdf.gz | 417.5 KB | Display | |
Data in XML | 1bdo_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 1bdo_validation.cif.gz | 7.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bd/1bdo ftp://data.pdbj.org/pub/pdb/validation_reports/bd/1bdo | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-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: BCCPSC IS OBTAINED BY DIGESTING RECOMBINANT BIOTIN CARBOXYL CARRIER PROTEIN WITH SUBTILISIN CARLSBERG Source: (gene. exp.) Escherichia coli (E. coli) Description: THE FRAGMENT BCCPSC, RESIDUES 77-156, IS OBTAINED BY DIGESTING THE EXPRESSED RECOMBINANT PROTEIN WITH SUBTILISIN CARLSBERG Gene: BIOTIN CARBOXYL CARRIER PROTEI / Plasmid: PRSETB / Gene (production host): BIOTIN CARBOXYL CARRIER PROTEIN / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PLYSS / References: UniProt: P0ABD8, acetyl-CoA carboxylase |
---|---|
#2: Chemical | ChemComp-BTN / |
#3: Water | ChemComp-HOH / |
Compound details | FUNCTIONAL CLASSIFICATION: BIOTIN CARBOXYL CARRIER PROTEIN BELONGS TO THE SUPERFAMILY OF BIOTINYL ...FUNCTIONAL |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 49 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal | *PLUS | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.9803 |
---|---|
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Aug 29, 1993 |
Radiation | Monochromator: CRYSTAL / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9803 Å / Relative weight: 1 |
Reflection | Num. obs: 14891 / % possible obs: 96.4 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.032 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 10 Å / Num. measured all: 28655 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: A MODIFIED MAD PROCEDURE. SOFTWARE USED : NULL STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL Resolution: 1.8→10 Å / σ(F): 2 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
|