+Open data
-Basic information
Entry | Database: PDB / ID: 2fae | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of E. coli decanoyl-ACP | ||||||
Components | Acyl carrier protein | ||||||
Keywords | BIOSYNTHETIC PROTEIN / acyl carrier protein / acyl chain binding / fatty acid biosynthesis | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||
Authors | Roujeinikova, A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal a Hydrophobic Binding Cavity that Can Expand to Fit Longer Substrates. Authors: Roujeinikova, A. / Simon, W.J. / Gilroy, J. / Rice, D.W. / Rafferty, J.B. / Slabas, A.R. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2fae.cif.gz | 52.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2fae.ent.gz | 36.4 KB | Display | PDB format |
PDBx/mmJSON format | 2fae.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2fae_validation.pdf.gz | 615.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2fae_full_validation.pdf.gz | 617.8 KB | Display | |
Data in XML | 2fae_validation.xml.gz | 12.1 KB | Display | |
Data in CIF | 2fae_validation.cif.gz | 17 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fa/2fae ftp://data.pdbj.org/pub/pdb/validation_reports/fa/2fae | HTTPS FTP |
-Related structure data
Related structure data | 2facC 2fadC 1l0iS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||||
2 |
| ||||||||||||||||||
3 |
| ||||||||||||||||||
4 |
| ||||||||||||||||||
5 |
| ||||||||||||||||||
6 |
| ||||||||||||||||||
7 |
| ||||||||||||||||||
8 |
| ||||||||||||||||||
9 |
| ||||||||||||||||||
10 |
| ||||||||||||||||||
11 |
| ||||||||||||||||||
Unit cell |
| ||||||||||||||||||
Components on special symmetry positions |
|
-Components
#1: Protein | Mass: 8514.264 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0A6A8 #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-PM8 / | #4: Chemical | ChemComp-PSE / | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.17 % |
---|---|
Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 8-12% PEG 4000, 30 mM zinc acetate, 50 mM sodium cocadylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→15 Å / Num. obs: 18488 / % possible obs: 86 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 12.6 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 17 |
Reflection shell | Resolution: 1.55→1.61 Å / Rmerge(I) obs: 0.311 / Mean I/σ(I) obs: 2.7 / Num. unique all: 1396 / % possible all: 67 |
-Processing
Software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB 1L0I Resolution: 1.55→10 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||
Solvent computation | Bsol: 76.755 Å2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.862 Å2
| ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→10 Å
| ||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||
Xplor file |
|