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Yorodumi- PDB-4drw: Crystal Structure of the Ternary Complex between S100A10, an Anne... -
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Basic information
| Entry | Database: PDB / ID: 4drw | ||||||
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| Title | Crystal Structure of the Ternary Complex between S100A10, an Annexin A2 N-terminal Peptide and an AHNAK Peptide | ||||||
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Keywords | EXOCYTOSIS/PROTEIN BINDING / ATYPICAL EF-HAND / HETEROPENTAMERIC COMPLEX / MEMBRANE REPAIR / EXOCYTOSIS-PROTEIN BINDING complex | ||||||
| Function / homology | Function and homology informationregulation of voltage-gated calcium channel activity / AnxA2-p11 complex / membrane raft assembly / positive regulation of receptor-mediated endocytosis involved in cholesterol transport / positive regulation of vacuole organization / phospholipase A2 inhibitor activity / positive regulation of low-density lipoprotein particle clearance / structural molecule activity conferring elasticity / positive regulation of vesicle fusion / myelin sheath adaxonal region ...regulation of voltage-gated calcium channel activity / AnxA2-p11 complex / membrane raft assembly / positive regulation of receptor-mediated endocytosis involved in cholesterol transport / positive regulation of vacuole organization / phospholipase A2 inhibitor activity / positive regulation of low-density lipoprotein particle clearance / structural molecule activity conferring elasticity / positive regulation of vesicle fusion / myelin sheath adaxonal region / negative regulation of low-density lipoprotein particle receptor catabolic process / positive regulation of plasma membrane repair / positive regulation of plasminogen activation / PCSK9-AnxA2 complex / cadherin binding involved in cell-cell adhesion / cornified envelope / cell-cell contact zone / Schmidt-Lanterman incisure / vesicle budding from membrane / plasma membrane protein complex / costamere / calcium-dependent phospholipid binding / osteoclast development / negative regulation of receptor internalization / Dissolution of Fibrin Clot / S100 protein binding / collagen fibril organization / vesicle membrane / epithelial cell apoptotic process / phosphatidylserine binding / regulation of RNA splicing / positive regulation of receptor recycling / basement membrane / positive regulation of exocytosis / positive regulation of GTPase activity / positive regulation of focal adhesion assembly / Smooth Muscle Contraction / regulation of neurogenesis / cytoskeletal protein binding / fibrinolysis / positive regulation of stress fiber assembly / phosphatidylinositol-4,5-bisphosphate binding / lipid droplet / positive regulation of substrate adhesion-dependent cell spreading / T-tubule / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / lung development / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / cell-matrix adhesion / response to activity / protein localization to plasma membrane / adherens junction / serine-type endopeptidase inhibitor activity / mRNA transcription by RNA polymerase II / sarcolemma / RNA polymerase II transcription regulator complex / nuclear matrix / calcium-dependent protein binding / azurophil granule lumen / late endosome membrane / melanosome / actin cytoskeleton / : / protease binding / midbody / angiogenesis / basolateral plasma membrane / vesicle / transmembrane transporter binding / early endosome / endosome / cadherin binding / lysosomal membrane / focal adhesion / calcium ion binding / Neutrophil degranulation / cell surface / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular space / RNA binding / extracellular exosome / extracellular region / identical protein binding / nucleus / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | ||||||
Authors | Rezvanpour, A. / Lee, T.-W. / Junop, M.S. / Shaw, G.S. | ||||||
Citation | Journal: Structure / Year: 2012Title: Structure of an asymmetric ternary protein complex provides insight for membrane interaction. Authors: Dempsey, B.R. / Rezvanpour, A. / Lee, T.W. / Barber, K.R. / Junop, M.S. / Shaw, G.S. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 4drw.cif.gz | 88.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4drw.ent.gz | 70.3 KB | Display | PDB format |
| PDBx/mmJSON format | 4drw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4drw_validation.pdf.gz | 473.4 KB | Display | wwPDB validaton report |
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| Full document | 4drw_full_validation.pdf.gz | 499.1 KB | Display | |
| Data in XML | 4drw_validation.xml.gz | 20.6 KB | Display | |
| Data in CIF | 4drw_validation.cif.gz | 26.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dr/4drw ftp://data.pdbj.org/pub/pdb/validation_reports/dr/4drw | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1bt6S 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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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 13765.778 Da / Num. of mol.: 4 Fragment: UNP P60903 residues 1-93 and UNP P07355 residues 2-16 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: S100A10, ANX2LG, CAL1L, CLP11 / Production host: ![]() #2: Protein/peptide | Mass: 2316.824 Da / Num. of mol.: 2 / Fragment: UNP Q09666 residues 5654-5673 / Source method: obtained synthetically / Details: CHEMICALLY SYNTHESIZED BASED ON HUMAN SEQUENCE / Source: (synth.) Homo sapiens (human) / References: UniProt: Q09666Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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Sample preparation
| Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.49 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM sodium chloride, 200mM magnesium chloride, 50mM sodium cacodylate, 20% PEG 1000, 0.15mM CYMAL-7, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 6, 2010 |
| Radiation | Monochromator: DOUBLE Si(111) CRYSTALS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
| Reflection | Resolution: 3.26→43.34 Å / Num. all: 7410 / Num. obs: 7306 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
| Reflection shell | Resolution: 3.26→3.32 Å / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 1BT6 Resolution: 3.5→43.34 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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| Refinement step | Cycle: LAST / Resolution: 3.5→43.34 Å
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| Refine LS restraints |
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Homo sapiens (human)
X-RAY DIFFRACTION
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