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Yorodumi- PDB-2bzr: Crystal structure of accD5 (Rv3280), an acyl-CoA carboxylase beta... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2bzr | |||||||||
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Title | Crystal structure of accD5 (Rv3280), an acyl-CoA carboxylase beta- subunit from Mycobacterium tuberculosis | |||||||||
Components | PROPIONYL-COA CARBOXYLASE BETA CHAIN 5 | |||||||||
Keywords | TRANSFERASE / MYCOBACTERIUM TUBERCULOSIS / FATTY ACID BIOSYNTHESIS / ACCASE / LIGASE / MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT / XMTB / STRUCTURAL GENOMICS | |||||||||
Function / homology | Function and homology information acetyl-CoA carboxytransferase / Transferases; Transferring one-carbon groups; Carboxy- and carbamoyltransferases / propionyl-CoA carboxylase activity / acetyl-CoA carboxylase complex / acetyl-CoA carboxylase activity / carbon fixation / cell wall / peptidoglycan-based cell wall / lipid metabolic process / transferase activity ...acetyl-CoA carboxytransferase / Transferases; Transferring one-carbon groups; Carboxy- and carbamoyltransferases / propionyl-CoA carboxylase activity / acetyl-CoA carboxylase complex / acetyl-CoA carboxylase activity / carbon fixation / cell wall / peptidoglycan-based cell wall / lipid metabolic process / transferase activity / protein-containing complex / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | MYCOBACTERIUM TUBERCULOSIS (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | |||||||||
Authors | Holton, S.J. | |||||||||
Citation | Journal: FEBS Lett. / Year: 2006 Title: Structural Diversity in the Six-Fold Redundant Set of Acyl-Coa Carboxyltransferases in Mycobacterium Tuberculosis. Authors: Holton, S.J. / King-Scott, S. / Eddine, A.N. / Kaufmann, S.H. / Wilmanns, M. | |||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bzr.cif.gz | 594.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bzr.ent.gz | 492.2 KB | Display | PDB format |
PDBx/mmJSON format | 2bzr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bz/2bzr ftp://data.pdbj.org/pub/pdb/validation_reports/bz/2bzr | 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 59361.938 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MYCOBACTERIUM TUBERCULOSIS (bacteria) / Strain: H37RV / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: P96885, UniProt: P9WQH7*PLUS, propionyl-CoA carboxylase #2: Water | ChemComp-HOH / | Compound details | HAS A CATALYTIC ACTIVITY | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.66 Å3/Da / Density % sol: 66.15 % |
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Crystal grow | pH: 7 / Details: pH 7.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.97889 |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97889 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→32.22 Å / Num. obs: 251643 / % possible obs: 96.4 % / Observed criterion σ(I): 0 / Redundancy: 4.79 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 13.27 |
Reflection shell | Resolution: 2.2→2.22 Å / Redundancy: 3.78 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 3.95 / % possible all: 78.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.2→32.09 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.926 / SU B: 3.984 / SU ML: 0.102 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.168 / ESU R Free: 0.153 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.7 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→32.09 Å
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Refine LS restraints |
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