+Open data
-Basic information
Entry | Database: PDB / ID: 1jbv | ||||||
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Title | FPGS-AMPPCP complex | ||||||
Components | FOLYLPOLYGLUTAMATE SYNTHASE | ||||||
Keywords | LIGASE / FPGS AMPPCP complex | ||||||
Function / homology | Function and homology information tetrahydrofolate synthase / tetrahydrofolylpolyglutamate synthase activity / one-carbon metabolic process / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Lactobacillus casei (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.95 Å | ||||||
Authors | Sun, X. / Cross, J.A. / Bognar, A.L. / Baker, E.N. / Smith, C.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Folate-binding triggers the activation of folylpolyglutamate synthetase. Authors: Sun, X. / Cross, J.A. / Bognar, A.L. / Baker, E.N. / Smith, C.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jbv.cif.gz | 100.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jbv.ent.gz | 73.5 KB | Display | PDB format |
PDBx/mmJSON format | 1jbv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jb/1jbv ftp://data.pdbj.org/pub/pdb/validation_reports/jb/1jbv | HTTPS FTP |
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-Related structure data
Related structure data | 1jbwC 1fgsS 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
#1: Protein | Mass: 46697.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lactobacillus casei (bacteria) / Plasmid: pCYB / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P15925, tetrahydrofolate synthase | ||||
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#2: Chemical | #3: Chemical | ChemComp-ACP / | #4: 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: 2.06 Å3/Da / Density % sol: 40.31 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.3 / Method: vapor diffusion, hanging dropDetails: Sun, X., (1998) Proc. Natl. Acad. Sci. USA, 95, 6647. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 10, 2000 / Details: mirrors |
Radiation | Monochromator: Mar mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→100 Å / Num. all: 28314 / Num. obs: 28314 / % possible obs: 94 % / Redundancy: 6.9 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 23.4 |
Reflection shell | Resolution: 1.9→1.97 Å / Rmerge(I) obs: 0.295 / Mean I/σ(I) obs: 3.2 / % possible all: 86.1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 100 Å / % possible obs: 94 % / Num. measured all: 195787 |
Reflection shell | *PLUS Highest resolution: 1.9 Å / % possible obs: 86.1 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FGS Resolution: 1.95→100 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.95→100 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 100 Å / % reflection Rfree: 5 % / Rfactor obs: 0.194 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |