+Open data
-Basic information
Entry | Database: PDB / ID: 6iqi | ||||||
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Title | crystal structure of Arabidopsis thaliana Profilin 2 | ||||||
Components | Profilin-2 | ||||||
Keywords | PLANT PROTEIN / actin binding / regulate actin network | ||||||
Function / homology | Function and homology information inflorescence development / lateral root development / leaf development / sequestering of actin monomers / actin polymerization or depolymerization / actin monomer binding / chloroplast / defense response / cell cortex / cytoskeleton ...inflorescence development / lateral root development / leaf development / sequestering of actin monomers / actin polymerization or depolymerization / actin monomer binding / chloroplast / defense response / cell cortex / cytoskeleton / endoplasmic reticulum / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Qiao, Z. / Gao, Y. | ||||||
Funding support | Singapore, 1items
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Citation | Journal: J.Biol.Chem. / Year: 2019 Title: Structural and computational examination of theArabidopsisprofilin-Poly-P complex reveals mechanistic details in profilin-regulated actin assembly. Authors: Qiao, Z. / Sun, H. / Ng, J.T.Y. / Ma, Q. / Koh, S.H. / Mu, Y. / Miao, Y. / Gao, Y.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6iqi.cif.gz | 115.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6iqi.ent.gz | 86 KB | Display | PDB format |
PDBx/mmJSON format | 6iqi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6iqi_validation.pdf.gz | 441.2 KB | Display | wwPDB validaton report |
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Full document | 6iqi_full_validation.pdf.gz | 446 KB | Display | |
Data in XML | 6iqi_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | 6iqi_validation.cif.gz | 14.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iq/6iqi ftp://data.pdbj.org/pub/pdb/validation_reports/iq/6iqi | HTTPS FTP |
-Related structure data
Related structure data | 6iqfC 6iqjC 6iqkC 3nulS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 14010.833 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: PRO2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q42418 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.98 Å3/Da / Density % sol: 58.69 % |
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Crystal grow | Temperature: 291.15 K / Method: evaporation Details: 0.1M Tris HCl (pH 8.5), 2.2M ammonium phosphate dibasic |
-Data collection
Diffraction | Mean temperature: 77 K / Serial crystal experiment: N |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-X / Wavelength: 1.54 Å |
Detector | Type: DECTRIS PILATUS 300K / Detector: PIXEL / Date: Mar 28, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→32.36 Å / Num. obs: 19448 / % possible obs: 98.91 % / Redundancy: 4.2 % / CC1/2: 0.996 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.3→2.38 Å / Num. unique obs: 719 / CC1/2: 0.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3NUL Resolution: 2.4→27.7 Å / Cross valid method: THROUGHOUT
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Displacement parameters | Biso mean: 64.53 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→27.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.48 Å
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