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Open data
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Basic information
Entry | Database: PDB / ID: 1l0i | ||||||
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Title | Crystal structure of butyryl-ACP I62M mutant | ||||||
![]() | Acyl carrier protein | ||||||
![]() | LIPID TRANSPORT / acyl carrier protein / acyl chain binding / fatty acid biosynthesis | ||||||
Function / homology | ![]() lipid biosynthetic process / lipid A biosynthetic process / phosphopantetheine binding / acyl binding / acyl carrier activity / fatty acid biosynthetic process / response to xenobiotic stimulus / lipid binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Roujeinikova, A. / Baldock, C. / Simon, W.J. / Gilroy, J. / Baker, P.J. / Stuitje, A.R. / Rice, D.W. / Slabas, A.R. / Rafferty, J.B. | ||||||
![]() | ![]() 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: ![]() 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). |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51.4 KB | Display | ![]() |
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PDB format | ![]() | 39.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.1 KB | Display | ![]() |
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Full document | ![]() | 443.3 KB | Display | |
Data in XML | ![]() | 4 KB | Display | |
Data in CIF | ![]() | 6.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 172 molecules ![](data/chem/img/NA.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/PSR.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/PSR.gif)
![](data/chem/img/HOH.gif)
#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: ![]() |
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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: ![]() ![]() ![]() |
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 % |
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Processing
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Refinement | Method to determine structure: ![]()
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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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