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Yorodumi- PDB-5cmo: Crystal structure of holo-[acyl-carrier-protein] synthase (AcpS) ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5cmo | ||||||
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Title | Crystal structure of holo-[acyl-carrier-protein] synthase (AcpS) from Neisseria meningitidis | ||||||
Components | Holo-[acyl-carrier-protein] synthase | ||||||
Keywords | TRANSFERASE / acpS / FASII / trimer | ||||||
Function / homology | Function and homology information holo-[acyl-carrier-protein] synthase / holo-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Neisseria meningitidis serogroup C / serotype 2a | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Nanson, J.D. / Forwood, J.K. | ||||||
Citation | Journal: To Be Published Title: Crystal structure of holo-[acyl-carrier-protein] synthase (AcpS) from Neisseria meningitidis Authors: Nanson, J.D. / Forwood, J.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5cmo.cif.gz | 232.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5cmo.ent.gz | 192.3 KB | Display | PDB format |
PDBx/mmJSON format | 5cmo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5cmo_validation.pdf.gz | 443.1 KB | Display | wwPDB validaton report |
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Full document | 5cmo_full_validation.pdf.gz | 445.7 KB | Display | |
Data in XML | 5cmo_validation.xml.gz | 18.2 KB | Display | |
Data in CIF | 5cmo_validation.cif.gz | 26 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cm/5cmo ftp://data.pdbj.org/pub/pdb/validation_reports/cm/5cmo | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13694.843 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) (bacteria) Strain: ATCC 700532 / DSM 15464 / FAM18 / Gene: acpS, NMC1700 / Plasmid: pMCSG21 / Production host: Escherichia coli (E. coli) References: UniProt: A1KVH5, holo-[acyl-carrier-protein] synthase #2: Chemical | ChemComp-GOL / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.82 % |
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Crystal grow | Temperature: 296.15 K / Method: vapor diffusion, hanging drop / Details: 200 mM sodium citrate tribasic, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 17, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2→48.06 Å / Num. obs: 28036 / % possible obs: 100 % / Redundancy: 7.2 % / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 7 % / Mean I/σ(I) obs: 3.4 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→46.522 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 22.03 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→46.522 Å
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Refine LS restraints |
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LS refinement shell |
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