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Yorodumi- PDB-1eqy: COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1eqy | ||||||
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Title | COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1 | ||||||
Components |
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Keywords | CONTRACTILE PROTEIN / gelsolin / actin | ||||||
Function / homology | Function and homology information striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding ...striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding / actin cap / regulation of podosome assembly / sequestering of actin monomers / myosin II binding / negative regulation of viral entry into host cell / actin filament severing / actin filament capping / actin filament depolymerization / actin polymerization or depolymerization / barbed-end actin filament capping / cell projection assembly / cardiac muscle cell contraction / podosome / Sensory processing of sound by outer hair cells of the cochlea / relaxation of cardiac muscle / cytoskeletal motor activator activity / cortical actin cytoskeleton / phagocytosis, engulfment / tropomyosin binding / mesenchyme migration / hepatocyte apoptotic process / troponin I binding / myosin heavy chain binding / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / actin monomer binding / sarcoplasm / cilium assembly / Caspase-mediated cleavage of cytoskeletal proteins / skeletal muscle fiber development / stress fiber / titin binding / phagocytic vesicle / phosphatidylinositol-4,5-bisphosphate binding / response to muscle stretch / actin filament polymerization / filopodium / central nervous system development / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / protein destabilization / cellular response to type II interferon / actin filament binding / calcium-dependent protein binding / actin cytoskeleton / lamellipodium / actin binding / cell body / secretory granule lumen / ficolin-1-rich granule lumen / amyloid fibril formation / blood microparticle / hydrolase activity / protein domain specific binding / Amyloid fiber formation / focal adhesion / calcium ion binding / Neutrophil degranulation / positive regulation of gene expression / magnesium ion binding / extracellular space / extracellular exosome / extracellular region / ATP binding / identical protein binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Oryctolagus cuniculus (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | McLaughlin, P.J. / Gooch, J.T. / Mannherz, H.G. / Weeds, A.G. | ||||||
Citation | Journal: Nature / Year: 1993 Title: Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Authors: McLaughlin, P.J. / Gooch, J.T. / Mannherz, H.G. / Weeds, A.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eqy.cif.gz | 123.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eqy.ent.gz | 98.3 KB | Display | PDB format |
PDBx/mmJSON format | 1eqy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1eqy_validation.pdf.gz | 469 KB | Display | wwPDB validaton report |
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Full document | 1eqy_full_validation.pdf.gz | 481.2 KB | Display | |
Data in XML | 1eqy_validation.xml.gz | 12.5 KB | Display | |
Data in CIF | 1eqy_validation.cif.gz | 22.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/1eqy ftp://data.pdbj.org/pub/pdb/validation_reports/eq/1eqy | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14060.871 Da / Num. of mol.: 1 / Fragment: DOMAIN 1 / Mutation: N33C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell: PLASMA / Plasmid: PMW172 / Production host: Escherichia coli (E. coli) / References: UniProt: P06396 | ||||
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#2: Protein | Mass: 42109.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: MUSCLE / References: UniProt: P68135 | ||||
#3: Chemical | #4: Chemical | ChemComp-ATP / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.32 Å3/Da / Density % sol: 62.94 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 6.6 Details: PEG 6000, sodium chloride, adenosine triphosphate, calcium, magnesium, sodium azide, pH 6.6, Vapor Diffusion, temperature 298.0K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.911 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 19, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.911 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→15.4 Å / Num. obs: 28998 / % possible obs: 89.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 31.5 Å2 / Rmerge(I) obs: 0.092 / Net I/σ(I): 5.7 |
Reflection shell | Resolution: 2.33→2.46 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.21 / % possible all: 66 |
Reflection shell | *PLUS % possible obs: 66 % |
-Processing
Software |
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Refinement | Resolution: 2.3→15.4 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→15.4 Å
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Refine LS restraints |
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