+Open data
-Basic information
Entry | Database: PDB / ID: 1w78 | ||||||
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Title | E.coli FolC in complex with DHPP and ADP | ||||||
Components | FOLC BIFUNCTIONAL PROTEIN | ||||||
Keywords | SYNTHASE / FOLC / DHFS / DIHYDROFOLATE SYNTHASE / ATP-BINDING / FOLATE BIOSYNTHESIS / LIGASE / MULTIFUNCTIONAL ENZYME | ||||||
Function / homology | Function and homology information dihydrofolate synthase / tetrahydrofolate synthase / dihydrofolate synthase activity / folic acid-containing compound biosynthetic process / tetrahydrofolylpolyglutamate synthase activity / folic acid biosynthetic process / guanosine tetraphosphate binding / tetrahydrofolate biosynthetic process / one-carbon metabolic process / ATP binding ...dihydrofolate synthase / tetrahydrofolate synthase / dihydrofolate synthase activity / folic acid-containing compound biosynthetic process / tetrahydrofolylpolyglutamate synthase activity / folic acid biosynthetic process / guanosine tetraphosphate binding / tetrahydrofolate biosynthetic process / one-carbon metabolic process / ATP binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.82 Å | ||||||
Authors | Mathieu, M. / Debousker, G. / Vincent, S. / Viviani, F. / Bamas-Jacques, N. / Mikol, V. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Escherichia Coli Folc Structure Reveals an Unexpected Dihydrofolate Binding Site Providing an Attractive Target for Anti-Microbial Therapy Authors: Mathieu, M. / Debousker, G. / Vincent, S. / Viviani, F. / Bamas-Jacques, N. / Mikol, V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1w78.cif.gz | 107.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1w78.ent.gz | 79.5 KB | Display | PDB format |
PDBx/mmJSON format | 1w78.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1w78_validation.pdf.gz | 511.8 KB | Display | wwPDB validaton report |
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Full document | 1w78_full_validation.pdf.gz | 517.6 KB | Display | |
Data in XML | 1w78_validation.xml.gz | 10 KB | Display | |
Data in CIF | 1w78_validation.cif.gz | 17.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w7/1w78 ftp://data.pdbj.org/pub/pdb/validation_reports/w7/1w78 | HTTPS FTP |
-Related structure data
Related structure data | 1w7kC 1jbvS C: citing same article (ref.) S: Starting model for refinement |
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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, 1 molecules A
#1: Protein | Mass: 45499.543 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PVRC1432 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): PVRC 1432 / References: UniProt: P08192, dihydrofolate synthase |
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-Non-polymers , 5 types, 495 molecules
#2: Chemical | ChemComp-PD8 / | ||||||
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#3: Chemical | #4: Chemical | ChemComp-SO4 / | #5: Chemical | ChemComp-ADP / | #6: Water | ChemComp-HOH / | |
-Details
Compound details | CATALYTIC ACTIVITY: ATP + DIHYDROPTE |
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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: 2.65 Å3/Da / Density % sol: 53.53 % |
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Crystal grow | pH: 8.7 Details: 1.5 M AMMONIUM SULFATE 5 MM DTT 50 MM BICINE PH 8.7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS / Wavelength: 1.5418 |
Detector | Type: MACSCIENCE DIP2000 / Detector: IMAGE PLATE / Date: Nov 6, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.82→25 Å / Num. obs: 42097 / % possible obs: 96.4 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 12.3 |
Reflection shell | Resolution: 1.82→1.92 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 3.7 / % possible all: 88.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1JBV Resolution: 1.82→25 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.82→25 Å
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