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Yorodumi- PDB-1kjj: Crystal structure of glycniamide ribonucleotide transformylase in... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1kjj | ||||||
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Title | Crystal structure of glycniamide ribonucleotide transformylase in complex with Mg-ATP-gamma-S | ||||||
Components | phosphoribosylglycinamide formyltransferase 2 | ||||||
Keywords | TRANSFERASE / ATP-grasp / purine biosynthesis / nucleotide | ||||||
Function / homology | Function and homology information phosphoribosylglycinamide formyltransferase 2 / phosphoribosylglycinamide formyltransferase 2 activity / acetate kinase activity / phosphoribosylglycinamide formyltransferase activity / 'de novo' IMP biosynthetic process / ligase activity / magnesium ion binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.75 Å | ||||||
Authors | Thoden, J.B. / Firestine, S.M. / Benkovic, S.J. / Holden, H.M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site. Authors: Thoden, J.B. / Firestine, S.M. / Benkovic, S.J. / Holden, H.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kjj.cif.gz | 179.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kjj.ent.gz | 138.1 KB | Display | PDB format |
PDBx/mmJSON format | 1kjj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kj/1kjj ftp://data.pdbj.org/pub/pdb/validation_reports/kj/1kjj | HTTPS FTP |
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-Related structure data
Related structure data | 1kj8C 1kj9C 1kjiC 1kjqC 1eyzS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 42349.340 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: PURT / Plasmid: pET-22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS References: UniProt: P33221, Transferases; Transferring one-carbon groups; Hydroxymethyl-, formyl- and related transferases |
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-Non-polymers , 6 types, 683 molecules
#2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-NA / | #4: Chemical | ChemComp-CL / | #5: Chemical | #6: Chemical | ChemComp-MPO / | #7: 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: 2.49 Å3/Da / Density % sol: 50.64 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: batch / pH: 6.7 Details: PEG 5000, NaCl, MgCl2, MOPS, ATP-gamma-S, pH 6.7, batch at 277K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: batch method / Details: used macroseeding | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54178 Å |
Detector | Type: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: Nov 6, 2000 / Details: goebel optics |
Radiation | Monochromator: goebel optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→30 Å / Num. all: 82695 / Num. obs: 82695 / % possible obs: 96 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 18.2 |
Reflection shell | Resolution: 1.75→1.87 Å / Redundancy: 1.4 % / Rmerge(I) obs: 0.215 / Mean I/σ(I) obs: 4.4 / Num. unique all: 9407 / % possible all: 88 |
Reflection | *PLUS Rmerge(I) obs: 0.06 |
Reflection shell | *PLUS % possible obs: 88 % / Num. unique obs: 9407 / Rmerge(I) obs: 0.215 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB ENTRY 1EYZ Resolution: 1.75→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.75→30 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor all: 0.187 / Rfactor Rfree: 0.233 / Rfactor Rwork: 0.184 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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