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- PDB-2c0r: CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2c0r | ||||||
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Title | CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR. ALKALOPHILUS AT pH 8.5 | ||||||
![]() | PHOSPHOSERINE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE / PHOSPHOSERINE AMINOTRANSFERASE / PYRIDOXAL-5'-PHOSPHATE / PYRIDINE SERINE BIOSYNTHESIS / AMINO-ACID BIOSYNTHESIS / AMINOTRANSFERASE / PYRIDOXAL PHOSPHATE / PYRIDOXINE BIOSYNTHESIS / SERINE BIOSYNTHESIS | ||||||
Function / homology | ![]() phosphoserine transaminase / O-phospho-L-serine:2-oxoglutarate aminotransferase activity / L-serine biosynthetic process / pyridoxal phosphate binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kapetaniou, E.G. / Papageorgiou, A.C. | ||||||
![]() | ![]() Title: Effect of Ph on the Structure and Stability of Bacillus Circulans Ssp. Alkalophilus Phosphoserine Aminotransferase: Thermodynamic and Crystallographic Studies. Authors: Kapetaniou, E.G. / Thanassoulas, A. / Dubnovitsky, A.P. / Nounesis, G. / Papageorgiou, A.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 318.4 KB | Display | ![]() |
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PDB format | ![]() | 259.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.8 KB | Display | ![]() |
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Full document | ![]() | 453.5 KB | Display | |
Data in XML | ![]() | 36.4 KB | Display | |
Data in CIF | ![]() | 55.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bjnS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99995, 0.0063, 0.0079), Vector: |
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Components
#1: Protein | Mass: 39966.090 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38 % |
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Crystal grow | pH: 8.5 Details: 30% PEG 4000, 0.1 M TRIS-HCL BUFFER, PH 8.5, 5% GLYCEROL, 0.2 M SODIUM ACETATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 4, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.81 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→15 Å / Num. obs: 171731 / % possible obs: 85.7 % / Observed criterion σ(I): 3 / Redundancy: 24.86 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 18.83 |
Reflection shell | Resolution: 1.2→1.24 Å / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 2.4 / % possible all: 74.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1BJN Resolution: 1.2→12 Å / Num. parameters: 57709 / Num. restraintsaints: 69730 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER / Details: ANISOTROPIC REFINEMENT
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Refine analyze | Num. disordered residues: 4 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 6397 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.2→12 Å
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Refine LS restraints |
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