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- PDB-6u6n: Structure of the trimeric globular domain of Adiponectin mutant -... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6u6n | ||||||
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Title | Structure of the trimeric globular domain of Adiponectin mutant - D187A Q188A | ||||||
![]() | Adiponectin | ||||||
![]() | HORMONE / globular domain | ||||||
Function / homology | ![]() negative regulation of intracellular protein transport / positive regulation of lipid transporter activity / positive regulation of metanephric podocyte development / positive regulation of renal albumin absorption / negative regulation of metanephric mesenchymal cell migration / response to linoleic acid / positive regulation of glycogen (starch) synthase activity / negative regulation of platelet-derived growth factor receptor-alpha signaling pathway / positive regulation of myeloid cell apoptotic process / negative regulation of macrophage differentiation ...negative regulation of intracellular protein transport / positive regulation of lipid transporter activity / positive regulation of metanephric podocyte development / positive regulation of renal albumin absorption / negative regulation of metanephric mesenchymal cell migration / response to linoleic acid / positive regulation of glycogen (starch) synthase activity / negative regulation of platelet-derived growth factor receptor-alpha signaling pathway / positive regulation of myeloid cell apoptotic process / negative regulation of macrophage differentiation / AMPK inhibits chREBP transcriptional activation activity / detection of oxidative stress / positive regulation of signal transduction / negative regulation of granulocyte differentiation / negative regulation of hormone secretion / negative regulation of protein autophosphorylation / low-density lipoprotein particle clearance / sialic acid binding / negative regulation of heterotypic cell-cell adhesion / negative regulation of vascular associated smooth muscle cell migration / response to sucrose / collagen trimer / negative regulation of low-density lipoprotein receptor activity / negative regulation of DNA biosynthetic process / positive regulation of monocyte chemotactic protein-1 production / negative regulation of platelet-derived growth factor receptor signaling pathway / negative regulation of synaptic transmission / positive regulation of cAMP-dependent protein kinase activity / negative regulation of phagocytosis / negative regulation of cold-induced thermogenesis / positive regulation of fatty acid metabolic process / negative regulation of fat cell differentiation / fatty acid beta-oxidation / positive regulation of protein kinase A signaling / fatty acid oxidation / negative regulation of vascular associated smooth muscle cell proliferation / negative regulation of macrophage derived foam cell differentiation / negative regulation of tumor necrosis factor production / regulation of glucose metabolic process / negative regulation of tumor necrosis factor-mediated signaling pathway / positive regulation of cholesterol efflux / response to tumor necrosis factor / negative regulation of gluconeogenesis / response to glucose / brown fat cell differentiation / negative regulation of canonical NF-kappaB signal transduction / cellular response to cAMP / response to glucocorticoid / cellular response to epinephrine stimulus / negative regulation of blood pressure / protein serine/threonine kinase activator activity / negative regulation of cell migration / response to nutrient / negative regulation of MAP kinase activity / negative regulation of receptor binding / response to activity / generation of precursor metabolites and energy / cytokine activity / positive regulation of interleukin-8 production / protein localization to plasma membrane / positive regulation of glucose import / response to bacterium / hormone activity / negative regulation of ERK1 and ERK2 cascade / negative regulation of inflammatory response / Transcriptional regulation of white adipocyte differentiation / circadian rhythm / cellular response to insulin stimulus / glucose metabolic process / positive regulation of peptidyl-tyrosine phosphorylation / cellular response to xenobiotic stimulus / glucose homeostasis / positive regulation of cold-induced thermogenesis / gene expression / positive regulation of canonical NF-kappaB signal transduction / response to ethanol / collagen-containing extracellular matrix / response to hypoxia / positive regulation of protein phosphorylation / signaling receptor binding / negative regulation of DNA-templated transcription / cell surface / endoplasmic reticulum / protein homodimerization activity / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pascolutti, R. / Kruse, A.C. / Erlandson, S.C. / Burri, D.J. / Zheng, S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Mapping and engineering the interaction between adiponectin and T-cadherin. Authors: Pascolutti, R. / Erlandson, S.C. / Burri, D.J. / Zheng, S. / Kruse, A.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.3 KB | Display | ![]() |
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PDB format | ![]() | 47.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.8 KB | Display | ![]() |
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Full document | ![]() | 427.4 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 8.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6u66SC S: Starting model for refinement C: citing same article ( |
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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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 16261.047 Da / Num. of mol.: 1 / Mutation: D187A, Q188A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CL / |
#3: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.86 Å3/Da / Density % sol: 33.98 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.2 M sodium nitrate, 0.1 M MES pH 5.5, 20% PEG 3350 PH range: 5-6 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 17, 2018 |
Radiation | Monochromator: Double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→50 Å / Num. obs: 29889 / % possible obs: 99.1 % / Redundancy: 5.3 % / Biso Wilson estimate: 47.68 Å2 / CC1/2: 0.99 / Rrim(I) all: 0.73 / Net I/σ(I): 12.42 |
Reflection shell | Resolution: 2.15→2.28 Å / Redundancy: 3.04 % / Mean I/σ(I) obs: 1.59 / Num. unique obs: 865 / CC1/2: 0.71 / Rrim(I) all: 0.66 / % possible all: 94.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6U66 Resolution: 2.15→39.18 Å / SU ML: 0.351 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 32.0923
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 68.12 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→39.18 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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