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- PDB-2xz1: The Structure of the 2:2 (Fully Occupied) Complex Between Stearoy... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xz1 | ||||||
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Title | The Structure of the 2:2 (Fully Occupied) Complex Between Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean) and Acyl Carrier Protein. | ||||||
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![]() | OXIDOREDUCTASE/LIPID BINDING PROTEIN / OXIDOREDUCTASE-LIPID BINDING PROTEIN COMPLEX | ||||||
Function / homology | ![]() stearoyl-[acyl-carrier-protein] 9-desaturase / : / stearoyl-[ACP] desaturase activity / stearoyl-CoA 9-desaturase activity / chloroplast stroma / phosphopantetheine binding / acyl carrier activity / chloroplast / fatty acid biosynthetic process / defense response ...stearoyl-[acyl-carrier-protein] 9-desaturase / : / stearoyl-[ACP] desaturase activity / stearoyl-CoA 9-desaturase activity / chloroplast stroma / phosphopantetheine binding / acyl carrier activity / chloroplast / fatty acid biosynthetic process / defense response / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guy, J.E. / Moche, M. / Whittle, E. / Lengqvist, J. / Shanklin, J. / Lindqvist, Y. | ||||||
![]() | ![]() Title: Remote Control of Regioselectivity in Acyl-Acyl Carrier Protein-Desaturases. Authors: Guy, J.E. / Whittle, E. / Moche, M. / Lengqvist, J. / Lindqvist, Y. / Shanklin, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 358.2 KB | Display | ![]() |
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PDB format | ![]() | 296.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2xz0C ![]() 1afrS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
-Protein , 2 types, 4 molecules ABCD
#1: Protein | Mass: 41703.312 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P22337, stearoyl-[acyl-carrier-protein] 9-desaturase #2: Protein | Mass: 8924.858 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: SER38 CHAIN D IS A PHOSPHOSERINE, IN CHAIN C IT IS ALSO LINKED TO A FRAGMENT OF PANTETHEINE Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 4 types, 9 molecules ![](data/chem/img/FE.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/PNY.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/PNY.gif)
#3: Chemical | ChemComp-FE / #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-PNY / ( | |
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-Details
Sequence details | SEQUENCE AS DESCRIBED IN BROADWATER |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.69 % / Description: NONE |
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Crystal grow | pH: 5.8 Details: 16-20% MPD,6-8% PEG20000, 0.1M SODIUM CACODYLATE PH 5.8, 4-6% ACETONITRILE |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 3.35→20 Å / Num. obs: 16101 / % possible obs: 92.7 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 9.7 |
Reflection shell | Resolution: 3.35→3.44 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.6 / Mean I/σ(I) obs: 2.7 / % possible all: 96 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1AFR Resolution: 3.35→20 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.931 / SU B: 60.836 / SU ML: 0.445 / Cross valid method: THROUGHOUT / ESU R Free: 0.585 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
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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: 107.329 Å2
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Refinement step | Cycle: LAST / Resolution: 3.35→20 Å
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Refine LS restraints |
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