+Open data
-Basic information
Entry | Database: PDB / ID: 1o17 | |||||||||
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Title | ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD) | |||||||||
Components | ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE | |||||||||
Keywords | TRANSFERASE / nucleoside-phosphorylases | |||||||||
Function / homology | Function and homology information anthranilate phosphoribosyltransferase / anthranilate phosphoribosyltransferase activity / tryptophan biosynthetic process / magnesium ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Sulfolobus solfataricus (archaea) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.05 Å | |||||||||
Authors | Mayans, O. / Ivens, A. / Kirschner, K. / Wilmanns, M. | |||||||||
Citation | Journal: Embo J. / Year: 2002 Title: Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry Authors: Mayans, O. / Ivens, A. / Nissen, L. / Kirschner, K. / Wilmanns, M. #1: Journal: Eur.J.Biochem. / Year: 2001 Title: Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus Authors: Ivens, A. / Mayans, O. / Szadkowski, H. / Wilmanns, M. / Kirschner, K. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1o17.cif.gz | 282.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1o17.ent.gz | 230.7 KB | Display | PDB format |
PDBx/mmJSON format | 1o17.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1o17_validation.pdf.gz | 444.5 KB | Display | wwPDB validaton report |
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Full document | 1o17_full_validation.pdf.gz | 495.6 KB | Display | |
Data in XML | 1o17_validation.xml.gz | 64.6 KB | Display | |
Data in CIF | 1o17_validation.cif.gz | 91.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o1/1o17 ftp://data.pdbj.org/pub/pdb/validation_reports/o1/1o17 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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Details | biological active form: dimer |
-Components
#1: Protein | Mass: 37619.516 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Production host: Escherichia coli (E. coli) / Strain (production host): KK8 References: UniProt: P50384, anthranilate phosphoribosyltransferase #2: Water | ChemComp-HOH / | |
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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: 2.24 Å3/Da / Density % sol: 45.16 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M HEPES pH7.0 or 0.05 M MES pH6.0 & 12-18% PEG 1500, VAPOR DIFFUSION, HANGING DROP at 293K, pH 6.5 | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7 / Details: Ivens, A., (2001) Eur.J.Biochem., 268, 2246. | ||||||||||||||||||||||||
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: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.834 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.834 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→18 Å / Num. obs: 77715 / % possible obs: 92.7 % / Redundancy: 3.6 % / Biso Wilson estimate: 27.2 Å2 / Rsym value: 0.053 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 2.05→2.09 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 1.8 / Num. unique all: 3382 / Rsym value: 0.245 / % possible all: 81.2 |
Reflection | *PLUS Rmerge(I) obs: 0.053 |
Reflection shell | *PLUS % possible obs: 81.2 % / Num. unique obs: 3382 / Rmerge(I) obs: 0.242 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.05→18 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.05→18 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rfree: 0.26 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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