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- PDB-1pne: CRYSTALLIZATION AND STRUCTURE DETERMINATION OF BOVINE PROFILIN AT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pne | ||||||
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Title | CRYSTALLIZATION AND STRUCTURE DETERMINATION OF BOVINE PROFILIN AT 2.0 ANGSTROMS RESOLUTION | ||||||
![]() | PROFILIN | ||||||
![]() | ACTIN BINDING PROTEIN | ||||||
Function / homology | ![]() PCP/CE pathway / RHO GTPases Activate Formins / positive regulation of actin filament bundle assembly / regulation of actin filament polymerization / actin binding / actin cytoskeleton organization / cytoskeleton / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Cedergren-Zeppezauer, E.S. / Goonesekere, N.C.W. / Rozycki, M.D. / Myslik, J.C. / Dauter, Z. / Lindberg, U. / Schutt, C.E. | ||||||
![]() | ![]() Title: Crystallization and structure determination of bovine profilin at 2.0 A resolution. Authors: Cedergren-Zeppezauer, E.S. / Goonesekere, N.C. / Rozycki, M.D. / Myslik, J.C. / Dauter, Z. / Lindberg, U. / Schutt, C.E. #1: ![]() Title: Structural Aspects of Actin-Binding Proteins Authors: Rozycki, M.D. / Myslik, J.C. / Schutt, C.E. / Lindberg, U. #2: ![]() Title: The Structure of Crystalline Profilin-Beta-Actin Authors: Schutt, C.E. / Myslik, J.C. / Rozycki, M.D. / Goonesekere, N.C.W. / Lindberg, U. #3: ![]() Title: Mutagenesis of Human Profilin Locates its Poly(L-Proline)-Binding Site to a Hydrophobic Patch of Aromatic Amino Acids Authors: Bjorkegren, C. / Rozycki, M. / Schutt, C.E. / Lindberg, U. / Karlsson, R. | ||||||
History |
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Remark 700 | SHEET PROFILIN IS DESCRIBED IN JRNL REFERENCE AS HAVING A 6-MEMBERED BETA-SHEET WHICH SHARES A ...SHEET PROFILIN IS DESCRIBED IN JRNL REFERENCE AS HAVING A 6-MEMBERED BETA-SHEET WHICH SHARES A STRAND WITH A SECOND 2-MEMBERED SHEET. TO CONFORM WITH PDB GUIDELINES, THESE SHEETS ARE COMBINED INTO A SINGLE 7-MEMBERED SHEET (SP1) IN THIS FILE. STRAND NUMBERING ALSO DIFFERS FROM THE JRNL REFERENCE. RESIDUES TRP 31 AND ILE 73 ADOPT BETA-BULGE CONFORMATIONS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.4 KB | Display | ![]() |
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PDB format | ![]() | 28.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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: 14968.185 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Compound details | GAMMA-TURN AT RESIDUES 25 - 27 DOES NOT HAVE THE CANONICAL I TO I+2 HYDROGEN BOND, SINCE CARBONYL O ...GAMMA-TURN AT RESIDUES 25 - 27 DOES NOT HAVE THE CANONICAL I TO I+2 HYDROGEN BOND, SINCE CARBONYL O OF LYS 25 IS HYDROGEN BONDED TO WATER MOLECULE 27. WATER MOLECULE 27 IS BONDED TO WATER MOLECULE 28, WHICH IN TURN IS BOUND TO THE CARBONYL O OF SER 27. THE INVOLVEMEN |
Sequence details | SEQUENCE IDENTIFIERS ARE NUMBERED 1 THROUGH 139 FOR STANDARD AMINO ACID RESIDUES. THE N-TERMINAL ...SEQUENCE IDENTIFIER |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.27 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Detector | Date: 1993 |
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Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 8239 / % possible obs: 95.9 % / Observed criterion σ(I): 2 / Redundancy: 3.56 % / Rmerge(I) obs: 0.066 |
Reflection | *PLUS Highest resolution: 2 Å / Num. measured all: 29297 / Rmerge(I) obs: 0.066 |
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Processing
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Refinement | Resolution: 2→6 Å / σ(F): 3 Details: RESIDUES ARE INCLUDED AT THE BEGINNING OF HELICES IF THEY PARTICIPATE IN HYDROGEN BONDING AND ARE "PARTIALLY" HELICAL, EVEN IF THE ENTIRE RESIDUE DOES NOT FIT HELICAL CRITERIA.
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Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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