+Open data
-Basic information
Entry | Database: PDB / ID: 2prf | ||||||
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Title | THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I | ||||||
Components | PROFILIN IA | ||||||
Keywords | ACTIN-BINDING | ||||||
Function / homology | Function and homology information actin monomer binding / actin cytoskeleton / actin cytoskeleton organization / cytoplasm Similarity search - Function | ||||||
Biological species | Acanthamoeba sp. (eukaryote) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Archer, S.J. / Vinson, V.K. / Pollard, T.D. / Lattman, E.E. / Torchia, D.A. | ||||||
Citation | Journal: J.Cell Biol. / Year: 1993 Title: Three-dimensional solution structure of Acanthamoeba profilin-I. Authors: Vinson, V.K. / Archer, S.J. / Lattman, E.E. / Pollard, T.D. / Torchia, D.A. #1: Journal: Biochemistry / Year: 1993 Title: Secondary Structure and Topology of Acanthamoeba Profilin I as Determined by Heteronuclear Nuclear Magnetic Resonance Spectroscopy Authors: Archer, S.J. / Vinson, V.K. / Pollard, T.D. / Torchia, D.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2prf.cif.gz | 676.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2prf.ent.gz | 560.9 KB | Display | PDB format |
PDBx/mmJSON format | 2prf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/2prf ftp://data.pdbj.org/pub/pdb/validation_reports/pr/2prf | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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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.) Acanthamoeba sp. (eukaryote) / References: UniProt: P07763, UniProt: P68696*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
NMR ensemble | Conformers submitted total number: 19 |