+Open data
-Basic information
Entry | Database: PDB / ID: 1l0i | ||||||
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Title | Crystal structure of butyryl-ACP I62M mutant | ||||||
Components | Acyl carrier protein | ||||||
Keywords | LIPID TRANSPORT / acyl carrier protein / acyl chain binding / fatty acid biosynthesis | ||||||
Function / homology | Function and homology information lipid A biosynthetic process / lipid biosynthetic process / phosphopantetheine binding / acyl binding / acyl carrier activity / fatty acid biosynthetic process / response to xenobiotic stimulus / lipid binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.2 Å | ||||||
Authors | Roujeinikova, A. / Baldock, C. / Simon, W.J. / Gilroy, J. / Baker, P.J. / Stuitje, A.R. / Rice, D.W. / Slabas, A.R. / Rafferty, J.B. | ||||||
Citation | Journal: Structure / Year: 2002 Title: X-ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site Authors: Roujeinikova, A. / Baldock, C. / Simon, W.J. / Gilroy, J. / Baker, P.J. / Stuitje, A.R. / Rice, D.W. / Slabas, A.R. / Rafferty, J.B. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2002 Title: Crystallisation and preliminary X-ray crystallographic studies on acyl-(acyl carrier protein) from Escherichia coli Authors: Roujeinikova, A. / Baldock, C. / Simon, W.J. / Gilroy, J. / Baker, P.J. / Stuitje, A.R. / Rice, D.W. / Rafferty, J.B. / Slabas, A.R. | ||||||
History |
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Remark 300 | Only the butryl, beta-mercaptoethylamine and phosphate moieties of the acylated 4' ...Only the butryl, beta-mercaptoethylamine and phosphate moieties of the acylated 4' phosphopantetheine group (PSR) attached to ACP were seen in the electron density. The rest of the 4' phosphopantetheine group was modelled in a stereochemically reasonable manner but omitted from the refinement process (occupancies set to 0.00). |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1l0i.cif.gz | 51.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1l0i.ent.gz | 39.4 KB | Display | PDB format |
PDBx/mmJSON format | 1l0i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l0/1l0i ftp://data.pdbj.org/pub/pdb/validation_reports/l0/1l0i | 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 8663.499 Da / Num. of mol.: 1 / Mutation: I62M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pET11D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0A6A8 |
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-Non-polymers , 5 types, 172 molecules
#2: Chemical | ChemComp-NA / | ||||||
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#3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-CAC / | #5: Chemical | ChemComp-PSR / | #6: 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: 2.1 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 4000, zinc acetate, sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Details: Roujeinikova, A., (2002) Acta Crystallogr., Sect.D, 58, 330. | ||||||||||||||||||||||||||||||
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: SRS / Beamline: PX14.2 / Wavelength: 0.978 Å |
Detector | Detector: CCD / Date: May 9, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→15 Å / Num. obs: 21956 / % possible obs: 92 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.086 |
Reflection shell | Resolution: 1.2→1.22 Å / Rmerge(I) obs: 0.391 / % possible all: 86 |
Reflection | *PLUS Highest resolution: 1.2 Å / Lowest resolution: 12 Å / % possible obs: 92 % / Num. measured all: 73325 |
Reflection shell | *PLUS % possible obs: 86 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.2→12 Å / Num. parameters: 7330 / Num. restraintsaints: 8289 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0
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Refinement step | Cycle: LAST / Resolution: 1.2→12 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.2 Å / Lowest resolution: 12 Å / % reflection Rfree: 5 % / Rfactor Rwork: 0.16 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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