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- PDB-1qls: S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qls | ||||||
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Title | S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS | ||||||
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![]() | METAL-BINDING PROTEIN/INHIBITOR / S100 FAMILY / EF-HAND PROTEIN / COMPLEX (LIGAND-ANNEXIN) / LIGAND OF ANNEXIN II / CALCIUM/PHOSPHOLIPID BINDING PROTEIN / METAL-BINDING PROTEIN-INHIBITOR complex | ||||||
Function / homology | ![]() regulation of interleukin-1 production / prolactin secretion / myoblast migration involved in skeletal muscle regeneration / regulation of leukocyte migration / granulocyte chemotaxis / positive regulation of T-helper 1 cell differentiation / phospholipase A2 inhibitor activity / regulation of hormone secretion / positive regulation of vesicle fusion / neutrophil clearance ...regulation of interleukin-1 production / prolactin secretion / myoblast migration involved in skeletal muscle regeneration / regulation of leukocyte migration / granulocyte chemotaxis / positive regulation of T-helper 1 cell differentiation / phospholipase A2 inhibitor activity / regulation of hormone secretion / positive regulation of vesicle fusion / neutrophil clearance / prostate gland development / negative regulation of T-helper 2 cell differentiation / positive regulation of neutrophil apoptotic process / endocrine pancreas development / positive regulation of prostaglandin biosynthetic process / negative regulation of interleukin-8 production / cadherin binding involved in cell-cell adhesion / peptide cross-linking / cornified envelope / Neutrophil degranulation / hepatocyte differentiation / neutrophil homeostasis / neutrophil activation / calcium-dependent phospholipid binding / gliogenesis / Formyl peptide receptors bind formyl peptides and many other ligands / negative regulation of exocytosis / motile cilium / S100 protein binding / cellular response to glucocorticoid stimulus / insulin secretion / DNA duplex unwinding / alpha-beta T cell differentiation / arachidonic acid secretion / positive regulation of cell migration involved in sprouting angiogenesis / positive regulation of wound healing / positive regulation of smooth muscle cell migration / phosphatidylserine binding / monocyte chemotaxis / phagocytic cup / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / response to X-ray / lateral plasma membrane / estrous cycle / Smooth Muscle Contraction / localization / cellular response to vascular endothelial growth factor stimulus / positive regulation of G1/S transition of mitotic cell cycle / phagocytosis / positive regulation of T cell proliferation / keratinocyte differentiation / ruffle / positive regulation of interleukin-2 production / response to interleukin-1 / adherens junction / phospholipid binding / sarcolemma / response to peptide hormone / cellular response to hydrogen peroxide / calcium-dependent protein binding / response to estradiol / regulation of cell population proliferation / regulation of cell shape / early endosome membrane / G alpha (i) signalling events / regulation of inflammatory response / actin cytoskeleton organization / G alpha (q) signalling events / basolateral plasma membrane / Interleukin-4 and Interleukin-13 signaling / collagen-containing extracellular matrix / adaptive immune response / vesicle / cell surface receptor signaling pathway / endosome / inflammatory response / apical plasma membrane / innate immune response / focal adhesion / signaling receptor binding / lipid binding / calcium ion binding / negative regulation of apoptotic process / cell surface / signal transduction / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rety, S. / Sopkova, J. / Renouard, M. / Osterloh, D. / Gerke, V. / Russo-Marie, F. / Lewit-Bentley, A. | ||||||
![]() | ![]() Title: Structural Basis of the Ca2+ Dependent Association between S100C (S100A11) and its Target, the N-Terminal Part of Annexin I Authors: Rety, S. / Osterloh, D. / Arie, J.P. / Tabaries, S. / Seeman, J. / Russo-Marie, F. / Gerke, V. / Lewit-Bentley, A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 36.7 KB | Display | ![]() |
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PDB format | ![]() | 24 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.2 KB | Display | ![]() |
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Full document | ![]() | 435.9 KB | Display | |
Data in XML | ![]() | 7.2 KB | Display | |
Data in CIF | ![]() | 8.6 KB | Display | |
Arichive directory | ![]() ![]() | 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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Unit cell |
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Details | BIOLOGICAL_UNIT: DIMERTHE DIMER IS COVALENT IN THE CRYSTAL, LINKED BY ADISULPHIDE AT CYS11. UNDER REDUCING CONDITIONS, THOUGHTHE DISULPHIDE WOULD BE REDUCED, THE DIMER SHOULD REMAININTACT.FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PERCHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR |
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Components
#1: Protein | Mass: 11194.829 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 1278.541 Da / Num. of mol.: 1 / Fragment: N-TERMINAL / Source method: obtained synthetically / Details: N-ACETYLATED ON N-TERMINUS / Source: (synth.) ![]() | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | SYNTHETIC ANNEXIN I N-TERMINAL SEQUENCE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.9 Å3/Da / Density % sol: 68.2 % | |||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 8.5 Details: 20 MG/ML PROTEIN WERE CRYSTALLIZED BY VAPOR DIFFUSION AGAINST 10% PEG 4000, 20% PEG 4000, 10% 2-PROPANOL, 100MM HEPES, PH=8.5, pH 8.50 | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: drop consists of 1:1 mixture of well and protein solutions | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 280 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 2, 1998 / Details: FOCUSSING MONOCHROMATOR |
Radiation | Monochromator: GE(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.37 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→69 Å / Num. obs: 9310 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Rmerge(I) obs: 0.08 / Rsym value: 0.08 / Net I/σ(I): 20.1 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 61772 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1BT6 Resolution: 2.3→20 Å / SU B: 4.869 / SU ML: 0.1216 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.217 / ESU R Free: 0.207
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Displacement parameters | Biso mean: 200.109 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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