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Open data
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Basic information
Entry | Database: PDB / ID: 1prq | ||||||
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Title | ACANTHAMOEBA CASTELLANII PROFILIN IA | ||||||
![]() | PROFILIN IA | ||||||
![]() | CONTRACTILE PROTEIN / ACTIN-BINDING PROTEIN | ||||||
Function / homology | ![]() sequestering of actin monomers / actin monomer binding / actin cytoskeleton / cell cortex / actin cytoskeleton organization Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Fedorov, A.A. / Pollard, T.D. / Way, M. / Lattman, E.E. / Almo, S.C. | ||||||
![]() | ![]() Title: Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii. Authors: Liu, S. / Fedorov, A.A. / Pollard, T.D. / Lattman, E.E. / Almo, S.C. / Magnus, K.A. #1: ![]() Title: The Molecular Basis for Allergen Cross-Reactivity: Crystal Structure and Ige-Epitope Mapping of Birch Pollen Profilin Authors: Fedorov, A.A. / Ball, T. / Mahoney, N.M. / Valenta, R. / Almo, S.C. #2: ![]() Title: X-Ray Structures of Isoforms of the Actin-Binding Protein Profilin that Differ in Their Affinity for Phosphatidylinositol Phosphates Authors: Fedorov, A.A. / Magnus, K.A. / Graupe, M.H. / Lattman, E.E. / Pollard, T.D. / Almo, S.C. #3: ![]() Title: Purification, Characterization and Crystallization of Acanthamoeba Profilin Expressed in Escherichia Coli Authors: Almo, S.C. / Pollard, T.D. / Way, M. / Lattman, E.E. #4: ![]() Title: Structure of Actin Binding Proteins: Insights About Function at Atomic Resolution Authors: Pollard, T.D. / Almo, S. / Quirk, S. / Vinson, V. / Lattman, E.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 35.1 KB | Display | ![]() |
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PDB format | ![]() | 24 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1acfS 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
#1: Protein | Mass: 12962.446 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 40 % |
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Crystal grow | pH: 8 / Details: 1.5 M SODIUM POTASSIUM TARTRATE, pH 8.0 |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1991 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→43.1 Å / Num. obs: 3255 / % possible obs: 82.76 % / Observed criterion σ(I): 2 / Redundancy: 2.9 % / Rmerge(I) obs: 0.049 / Net I/σ(I): 19.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: REFINED ACANTHAMOEBA PROFILIN IB STRUCTURE (1ACF) Resolution: 2.5→8 Å / σ(F): 2
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Refine analyze | Luzzati coordinate error obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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