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- PDB-2v8g: Crystal structure of beta-alanine synthase from Saccharomyces klu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2v8g | ||||||
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Title | Crystal structure of beta-alanine synthase from Saccharomyces kluyveri in complex with the product beta-alanine | ||||||
![]() | BETA-ALANINE SYNTHASE![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lundgren, S. / Andersen, B. / Piskur, J. / Dobritzsch, D. | ||||||
![]() | ![]() Title: Crystal Structures of Yeast -Alanine Synthase Complexes Reveal the Mode of Substrate Binding and Large Scale Domain Closure Movements. Authors: Lundgren, S. / Andersen, B. / Piskur, J. / Dobritzsch, D. #1: ![]() Title: Yeast Beta-Alanine Synthase Shares a Structural Scaffold and Origin with Dizinc-Dependent Exopeptidases Authors: Lundgren, S. / Gojkovic, Z. / Piskur, J. / Dobritzsch, D. #2: Journal: Acta Crystallogr.,Sect.D / Year: 2003 Title: Crystallization and Preliminary X-Ray Analysis of Beta-Alanine Synthase from the Yeast Saccharomyces Kluyveri Authors: Dobritzsch, D. / Gojkovic, Z. / Andersen, B. / Piskur, J. | ||||||
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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 335.7 KB | Display | ![]() |
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PDB format | ![]() | 272.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2v8dC ![]() 2v8hC ![]() 2v8vC ![]() 1r43S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1 / Refine code: 2
NCS oper:
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Components
#1: Protein | ![]() Mass: 52006.809 Da / Num. of mol.: 4 / Fragment: RESIDUES 2-455 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | ![]() #4: Chemical | ChemComp-BCN / ![]() #5: Water | ChemComp-HOH / | ![]() Sequence details | THE N-TERMINAL METHIONINE IS ABSENT, MOST LIKELY DUE TO POSTTRANSLATIONAL MODIFICATION. THE LAST 20 ...THE N-TERMINAL METHIONINE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 41 % / Description: NONE |
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Crystal grow![]() | pH: 8.75 / Details: PEG 6000, TRIS PH 8.5, BICINE PH 9.0, LICL. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Mar 13, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.5→20 Å / Num. obs: 59732 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 4.9 % / Rmerge(I) obs: 0.16 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 2.5→2.6 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 5.29 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1R43 Resolution: 2.5→19.84 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.902 / SU B: 19.409 / SU ML: 0.21 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 1.242 / ESU R Free: 0.289 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.36 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→19.84 Å
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Refine LS restraints |
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