+Open data
-Basic information
Entry | Database: PDB / ID: 1f1o | ||||||
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Title | STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES | ||||||
Components | ADENYLOSUCCINATE LYASE | ||||||
Keywords | LYASE / purine biosynthesis | ||||||
Function / homology | Function and homology information AMP biosynthetic process / adenylosuccinate lyase / N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity / (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity / 'de novo' AMP biosynthetic process / 'de novo' IMP biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.25 Å | ||||||
Authors | Toth, E.A. / Yeates, T. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. Authors: Toth, E.A. / Worby, C. / Dixon, J.E. / Goedken, E.R. / Marqusee, S. / Yeates, T.O. | ||||||
History |
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Remark 99 | The coordinate section in this entry contains CA atoms only |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f1o.cif.gz | 24.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f1o.ent.gz | 12.5 KB | Display | PDB format |
PDBx/mmJSON format | 1f1o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f1/1f1o ftp://data.pdbj.org/pub/pdb/validation_reports/f1/1f1o | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 49553.734 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P12047, adenylosuccinate lyase |
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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: 6.89 Å3/Da | ||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.8 Details: 0.1 M MES, 1.5 M ammonium sulfate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 47.7 % | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃Details: This particular structure is not described in this paper. pH: 5 | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3.25→50 Å / Num. all: 22850 / Num. obs: 2843 / % possible obs: 87.6 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.058 |
Reflection | *PLUS Num. measured all: 22850 |
-Processing
Software |
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Refinement | Resolution: 3.25→50 Å / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3.25→50 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM | ||||||||||||||||||||
Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 50 Å | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |