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Open data
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Basic information
Entry | Database: PDB / ID: 8h1w | ||||||
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Title | Serine Palmitoyltransferase from Sphingobacterium multivorum | ||||||
![]() | Serine palmitoyltransferase | ||||||
![]() | TRANSFERASE / sphingolipid | ||||||
Function / homology | ![]() 8-amino-7-oxononanoate synthase activity / serine C-palmitoyltransferase activity / serine C-palmitoyltransferase / sphingosine biosynthetic process / ceramide biosynthetic process / pyridoxal phosphate binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Takahashi, A. / Murakami, T. / Katayama, A. / Miyahara, I. / Kamiya, N. / Ikushiro, H. / Yano, T. | ||||||
Funding support | 1items
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![]() | ![]() Title: Structural insights into the substrate recognition of serine palmitoyltransferase from Sphingobacterium multivorum. Authors: Ikushiro, H. / Murakami, T. / Takahashi, A. / Katayama, A. / Sawai, T. / Goto, H. / Koolath, S. / Murai, Y. / Monde, K. / Miyahara, I. / Kamiya, N. / Yano, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 114 KB | Display | ![]() |
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PDB format | ![]() | 82.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.6 KB | Display | ![]() |
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Full document | ![]() | 447.3 KB | Display | |
Data in XML | ![]() | 22.9 KB | Display | |
Data in CIF | ![]() | 35.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8h1qC ![]() 8h1yC ![]() 8h20C ![]() 8h21C ![]() 8h29C ![]() 3a2bS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 44050.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-EDO / #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.19 % |
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Crystal grow | Temperature: 297 K / Method: vapor diffusion, sitting drop / Details: PEG4000, sodium acetate, Tris-HCl |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX225-HS / Detector: CCD / Date: Dec 11, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→50 Å / Num. obs: 80227 / % possible obs: 100 % / Redundancy: 10.8 % / CC1/2: 1 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 1.4→1.48 Å / Num. unique obs: 12715 / CC1/2: 0.848 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3A2B Resolution: 1.4→43.604 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.967 / SU B: 1.331 / SU ML: 0.051 / Cross valid method: FREE R-VALUE / ESU R: 0.064 / ESU R Free: 0.068 Details: Hydrogens have been added in their riding positions
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.099 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→43.604 Å
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Refine LS restraints |
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LS refinement shell |
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