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- PDB-3zvu: Structure of the PYR1 His60Pro mutant in complex with the HAB1 ph... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3zvu | ||||||
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Title | Structure of the PYR1 His60Pro mutant in complex with the HAB1 phosphatase and Abscisic acid | ||||||
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![]() | RECEPTOR/HYDROLASE / RECEPTOR-HYDROLASE COMPLEX / HORMONE RECEPTOR / STRESS RESPONSE | ||||||
Function / homology | ![]() positive regulation of response to water deprivation / regulation of protein serine/threonine phosphatase activity / plant-type vacuole membrane / protein phosphatase inhibitor complex / abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase ...positive regulation of response to water deprivation / regulation of protein serine/threonine phosphatase activity / plant-type vacuole membrane / protein phosphatase inhibitor complex / abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / ubiquitin-like protein ligase binding / signaling receptor activity / protein homodimerization activity / identical protein binding / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Betz, K. / Dupeux, F. / Santiago, J. / Rodriguez, P.L. / Marquez, J.A. | ||||||
![]() | ![]() Title: A Thermodynamic Switch Modulates Abscisic Acid Receptor Sensitivity. Authors: Dupeux, F. / Santiago, J. / Betz, K. / Twycross, J. / Park, S. / Rodriguez, L. / Gonzalez-Guzman, M. / Jensen, M.R. / Krasnogor, N. / Blackledge, M. / Holdsworth, M. / Cutler, S.R. / ...Authors: Dupeux, F. / Santiago, J. / Betz, K. / Twycross, J. / Park, S. / Rodriguez, L. / Gonzalez-Guzman, M. / Jensen, M.R. / Krasnogor, N. / Blackledge, M. / Holdsworth, M. / Cutler, S.R. / Rodriguez, P.L. / Marquez, J.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 | ![]() | 115.3 KB | Display | ![]() |
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PDB format | ![]() | 85.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 468.7 KB | Display | ![]() |
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Full document | ![]() | 476.9 KB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 30.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3qn1S S: Starting model for refinement |
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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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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 21664.307 Da / Num. of mol.: 1 / Fragment: RESIDUES 3-191 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 37347.824 Da / Num. of mol.: 1 Fragment: HAB1 PHOSPHATASE CATALYTIC REGION, RESIDUES 178-511 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9CAJ0, protein-serine/threonine phosphatase |
-Non-polymers , 4 types, 211 molecules ![](data/chem/img/A8S.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-A8S / ( | ||||
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#4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
-Details
Sequence details | CHAIN A VARIANT WAS GENERATED FROM SWISS-PROT ENTRY O49686.1. CHAIN B SEQUENCE WAS GENERATED FROM ...CHAIN A VARIANT WAS GENERATED FROM SWISS-PROT ENTRY O49686.1. CHAIN B SEQUENCE WAS GENERATED FROM GENBANK ENTRY AEE35372.1. |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.39 % / Description: NONE |
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Crystal grow | Temperature: 293 K / pH: 7.5 / Details: 0.25M AMSO4, 19% PEG 3350 AT 20 DEG. C, pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 3, 2011 / Details: SILICON TOROIDAL MIRROR COATED WITH RHODIUM |
Radiation | Monochromator: SILICON (1 1 1) CHANNEL- CUT / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97924 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→24.29 Å / Num. obs: 31132 / % possible obs: 99.7 % / Observed criterion σ(I): 2 / Redundancy: 7.14 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 19.7 |
Reflection shell | Resolution: 2.2→2.21 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 4.42 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3QN1 Resolution: 2.1→24.29 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.931 / SU B: 4.88 / SU ML: 0.128 / Cross valid method: THROUGHOUT / ESU R: 0.206 / ESU R Free: 0.184 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES REFINED INDIVIDUALLY.
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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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.807 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→24.29 Å
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Refine LS restraints |
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