+Open data
-Basic information
Entry | Database: PDB / ID: 1q8x | ||||||
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Title | NMR structure of human cofilin | ||||||
Components | Cofilin, non-muscle isoformADF/Cofilin family | ||||||
Keywords | STRUCTURAL PROTEIN / ADF/cofilin / chemical shift perturbation / actin cytoskeleton / G-actin binding | ||||||
Function / homology | Function and homology information actin filament fragmentation / positive regulation of embryonic development / establishment of spindle localization / positive regulation by host of viral process / actin filament severing / regulation of dendritic spine morphogenesis / actin filament depolymerization / RHO GTPases Activate ROCKs / regulation of cell morphogenesis / lamellipodium membrane ...actin filament fragmentation / positive regulation of embryonic development / establishment of spindle localization / positive regulation by host of viral process / actin filament severing / regulation of dendritic spine morphogenesis / actin filament depolymerization / RHO GTPases Activate ROCKs / regulation of cell morphogenesis / lamellipodium membrane / mitotic cytokinesis / Rho protein signal transduction / Sema3A PAK dependent Axon repulsion / cytoskeleton organization / EPHB-mediated forward signaling / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / response to virus / Regulation of actin dynamics for phagocytic cup formation / ruffle membrane / nuclear matrix / actin filament binding / actin cytoskeleton / Platelet degranulation / lamellipodium / growth cone / actin cytoskeleton organization / vesicle / focal adhesion / negative regulation of apoptotic process / extracellular space / extracellular exosome / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | Pope, B.J. / Zierler-Gould, K.M. / Kuhne, R. / Weeds, A.G. / Ball, L.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: The solution structure of human cofilin: rationalizing actin binding and pH sensitivity Authors: Pope, B.J. / Zierler-Gould, K.M. / Kuhne, R. / Weeds, A.G. / Ball, L.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1q8x.cif.gz | 1017.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1q8x.ent.gz | 882.9 KB | Display | PDB format |
PDBx/mmJSON format | 1q8x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q8/1q8x ftp://data.pdbj.org/pub/pdb/validation_reports/q8/1q8x | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 18532.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CFL1 OR CFL / Plasmid: pMW172 / Production host: Escherichia coli (E. coli) / Strain (production host): BL27(DE3) / References: UniProt: P23528 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |