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Open data
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Basic information
Entry | Database: PDB / ID: 2uuv | ||||||
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Title | alkyldihydroxyacetonephosphate synthase in P1 | ||||||
![]() | ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE | ||||||
![]() | TRANSFERASE / RHIZOMELIC CHONDRODYSPLASIA PUNCTATA / BIOSYNTHESIS OF PHOSPHOLIPIDS / FLAVOPROTEIN / LIPID SYNTHESIS / PEROXISOMAL DISORDER / FAD / FLAVIN / PEROXISOME / PLASMALOGENS | ||||||
Function / homology | ![]() alcohol binding / alkylglycerone-phosphate synthase / alkylglycerone-phosphate synthase activity / ether lipid biosynthetic process / FAD binding / peroxisome / flavin adenine dinucleotide binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Razeto, A. / Mattiroli, F. / Carpanelli, E. / Aliverti, A. / Pandini, V. / Coda, A. / Mattevi, A. | ||||||
![]() | ![]() Title: The Crucial Step in Ether Phospholipid Biosynthesis: Structural Basis of a Noncanonical Reaction Associated with a Peroxisomal Disorder. Authors: Razeto, A. / Mattiroli, F. / Carpanelli, E. / Aliverti, A. / Pandini, V. / Coda, A. / Mattevi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 447.4 KB | Display | ![]() |
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PDB format | ![]() | 365.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 91.2 KB | Display | |
Data in CIF | ![]() | 127.8 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 66104.734 Da / Num. of mol.: 4 / Fragment: RESIDUES 9-587 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: ACADEMIA DNA SEQUENCING CENTER IN COLLABORATION WITH DICTYOSTELIUM CDNA PROJECT Plasmid: PET28A / Production host: ![]() ![]() References: UniProt: O96759, alkylglycerone-phosphate synthase #2: Chemical | ChemComp-FAD / #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE GIVEN CORRESPONDS TO THE CONSTRUCT (9-587) WITH THE ADDITIONAL AA AT THE N-TERM GAMGS ...THE SEQUENCE GIVEN CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.53 % |
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Crystal grow | Details: 12% PEG4K, 200MM LI2SO4, 100MM TRISCL PH=8.5 |
-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jun 27, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2→48.4 Å / Num. obs: 176351 / % possible obs: 95.3 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.4 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 3.4 / % possible all: 89 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: MAXIMUM LIKELIHOODWITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.95 Å2
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Refinement step | Cycle: LAST / Resolution: 1.99→19.98 Å
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Refine LS restraints |
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