+Open data
-Basic information
Entry | Database: PDB / ID: 4bt6 | ||||||
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Title | acetolactate decarboxylase with a bound glycerol | ||||||
Components | ALPHA-ACETOLACTATE DECARBOXYLASE | ||||||
Keywords | LYASE / ACETOIN BIOSYNTHESIS / STEREOSELECTIVE DECARBOXYLATION / BIFUNCTIONAL ENZYME | ||||||
Function / homology | Function and homology information acetolactate decarboxylase / acetoin biosynthetic process / acetolactate decarboxylase activity Similarity search - Function | ||||||
Biological species | BREVIBACILLUS BREVIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | A Marlow, V. / Rea, D. / Najmudin, S. / Wills, M. / Fulop, V. | ||||||
Citation | Journal: Acs Chem.Biol. / Year: 2013 Title: Structure and Mechanism of Acetolactate Decarboxylase. Authors: Marlow, V.A. / Rea, D. / Najmudin, S. / Wills, M. / Fulop, V. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4bt6.cif.gz | 112.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4bt6.ent.gz | 86.8 KB | Display | PDB format |
PDBx/mmJSON format | 4bt6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4bt6_validation.pdf.gz | 431.8 KB | Display | wwPDB validaton report |
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Full document | 4bt6_full_validation.pdf.gz | 432.4 KB | Display | |
Data in XML | 4bt6_validation.xml.gz | 14.6 KB | Display | |
Data in CIF | 4bt6_validation.cif.gz | 22.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/4bt6 ftp://data.pdbj.org/pub/pdb/validation_reports/bt/4bt6 | HTTPS FTP |
-Related structure data
Related structure data | 4bt2SC 4bt3C 4bt4C 4bt5C 4bt7C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-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: 28830.621 Da / Num. of mol.: 1 / Fragment: RESIDUES 29-285 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BREVIBACILLUS BREVIS (bacteria) / Plasmid: PJA199 / Production host: BACILLUS SUBTILIS (bacteria) / Strain (production host): JA222 / Variant (production host): TOC46 / References: UniProt: P23616, acetolactate decarboxylase | ||
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#2: Chemical | ChemComp-ZN / | ||
#3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44 % / Description: NONE |
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Crystal grow | pH: 8.5 Details: 0.2 M TRIMETHYLAMINE N-OXIDE (TMAO), 0.1 M TRIS PH 8.5, 28-33 PEG 2K MME |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SEALED TUBE / Type: Xenocs GeniX 3D Cu HF / Wavelength: 1.5418 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 18, 2011 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→41 Å / Num. obs: 34655 / % possible obs: 99.1 % / Observed criterion σ(I): -3 / Redundancy: 13.9 % / Biso Wilson estimate: 9.9 Å2 / Rmerge(I) obs: 0.18 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 12.2 % / Rmerge(I) obs: 1.01 / Mean I/σ(I) obs: 3.4 / % possible all: 94.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4BT2 Resolution: 1.6→40.82 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.925 / SU B: 3.31 / SU ML: 0.054 / Cross valid method: THROUGHOUT / ESU R: 0.084 / ESU R Free: 0.09 / 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 / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.317 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→40.82 Å
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Refine LS restraints |
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