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Yorodumi- PDB-1bjo: THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bjo | ||||||
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Title | THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE | ||||||
Components | (PHOSPHOSERINE AMINOTRANSFERASE) x 2 | ||||||
Keywords | AMINOTRANSFERASE / L-SERINE BIOSYNTHESIS | ||||||
Function / homology | Function and homology information lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate / phosphoserine transaminase / O-phospho-L-serine:2-oxoglutarate aminotransferase activity / pyridoxal phosphate biosynthetic process / pyridoxine biosynthetic process / L-serine metabolic process / L-serine biosynthetic process / pyridoxal phosphate binding / protein homodimerization activity / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / DIFFERENCE FOURIER / Resolution: 2.8 Å | ||||||
Authors | Hester, G. / Stark, W. / Jansonius, J.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate. Authors: Hester, G. / Stark, W. / Moser, M. / Kallen, J. / Markovic-Housley, Z. / Jansonius, J.N. #1: Journal: Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors: Proceedings of the 8Th International Symposium on Vitamin B6 and Carbonyl Catalysis Year: 1991 Title: The Three Dimensional Structure of Phosphoserine Aminotransferase from Escherichia Coli Authors: Stark, W. / Kallen, J. / Markovic-Housley, Z. / Fol, B. / Kania, M. / Jansonius, J.N. #2: Journal: Biochemistry of Vitamin B6: Proceedings of the 7Th International Congress on Chemical and Biological Aspects of Vitamin B6 Catalysis (in: Iub Symp. Ser., V.166) Year: 1987 Title: Crystallographic and Solution Studies on Phosphoserine Aminotransferase (Psat) from E. Coli Authors: Kallen, J. / Kania, M. / Markovic-Housley, Z. / Vincent, M.G. / Jansonius, J.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bjo.cif.gz | 135 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bjo.ent.gz | 111.9 KB | Display | PDB format |
PDBx/mmJSON format | 1bjo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bjo_validation.pdf.gz | 462.1 KB | Display | wwPDB validaton report |
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Full document | 1bjo_full_validation.pdf.gz | 466.8 KB | Display | |
Data in XML | 1bjo_validation.xml.gz | 26.8 KB | Display | |
Data in CIF | 1bjo_validation.cif.gz | 36.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bj/1bjo ftp://data.pdbj.org/pub/pdb/validation_reports/bj/1bjo | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.45212, -0.73722, 0.50209), Vector: |
-Components
#1: Protein | Mass: 39709.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: IN CHAIN A AN EXTERNAL ALDIMINE INTERMEDIATE BETWEEN PYRIDOXAL-5'-PHOSPHATE AND ALPHA-METHYL-L-GLUTAMATE IS NON-COVALENTLY BOUND WHILE IN CHAIN B A PYRIDOXAL-5'-PHOSPHATE MOLECULE IS ...Details: IN CHAIN A AN EXTERNAL ALDIMINE INTERMEDIATE BETWEEN PYRIDOXAL-5'-PHOSPHATE AND ALPHA-METHYL-L-GLUTAMATE IS NON-COVALENTLY BOUND WHILE IN CHAIN B A PYRIDOXAL-5'-PHOSPHATE MOLECULE IS COVALENTLY BOUND IN AN ALDIMINE LINKAGE TO A LYSINE SIDE CHAIN Source: (gene. exp.) Escherichia coli (E. coli) / Gene: SERC References: PIR: S28806, UniProt: P23721*PLUS, phosphoserine transaminase |
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#2: Protein | Mass: 39937.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: IN CHAIN A AN EXTERNAL ALDIMINE INTERMEDIATE BETWEEN PYRIDOXAL-5'-PHOSPHATE AND ALPHA-METHYL-L-GLUTAMATE IS NON-COVALENTLY BOUND WHILE IN CHAIN B A PYRIDOXAL-5'-PHOSPHATE MOLECULE IS ...Details: IN CHAIN A AN EXTERNAL ALDIMINE INTERMEDIATE BETWEEN PYRIDOXAL-5'-PHOSPHATE AND ALPHA-METHYL-L-GLUTAMATE IS NON-COVALENTLY BOUND WHILE IN CHAIN B A PYRIDOXAL-5'-PHOSPHATE MOLECULE IS COVALENTLY BOUND IN AN ALDIMINE LINKAGE TO A LYSINE SIDE CHAIN Source: (gene. exp.) Escherichia coli (E. coli) / Gene: SERC References: PIR: S28806, UniProt: P23721*PLUS, phosphoserine transaminase |
#3: Chemical | ChemComp-PLP / |
#4: Chemical | ChemComp-GAM / |
#5: 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: 2.7 Å3/Da / Density % sol: 52 % | ||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: PSAT HAS BEEN CRYSTALLIZED AT 4-7 DEGREES CELSIUS BY THE HANGING DROP METHOD, USING PEG4000 AS A PRECIPITANT, BUFFERED WITH SODIUM ACETATE TO PH 7.2 IN THE DROP AND PH 5.6 IN THE RESERVOIR. ...Details: PSAT HAS BEEN CRYSTALLIZED AT 4-7 DEGREES CELSIUS BY THE HANGING DROP METHOD, USING PEG4000 AS A PRECIPITANT, BUFFERED WITH SODIUM ACETATE TO PH 7.2 IN THE DROP AND PH 5.6 IN THE RESERVOIR. THE PH-GRADIENT WAS ESSENTIAL FOR THE CRYSTALLIZATION., vapor diffusion - hanging drop, temperature 277K PH range: 5.6-7.2 | ||||||||||||
Crystal grow | *PLUS Temperature: 4-7 ℃ / Method: vapor diffusion, hanging drop / Details: pH7.2 in the drop and pH5.6 in the reservoir | ||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-20 / Wavelength: 1.5418 |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Jul 1, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→39.8 Å / Num. obs: 19908 / % possible obs: 91.8 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Biso Wilson estimate: 45.4 Å2 / Rsym value: 0.094 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 1.8 % / Mean I/σ(I) obs: 2.8 / Rsym value: 0.402 / % possible all: 68.4 |
Reflection | *PLUS Rmerge(I) obs: 0.094 / Biso Wilson estimate: 29.1 Å2 |
Reflection shell | *PLUS % possible obs: 68.4 % / Rmerge(I) obs: 0.402 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER / Resolution: 2.8→39.8 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: GROUP / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
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Displacement parameters | Biso mean: 33.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→39.8 Å
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Refine LS restraints |
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Refine LS restraints NCS | Rms dev Biso : 1.5 Å2 / Rms dev position: 0.48 Å / Weight position: 500 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.8→2.9 Å / Rfactor Rfree error: 0.05 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.315 |