+Open data
-Basic information
Entry | Database: PDB / ID: 2ao7 | ||||||
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Title | Adam10 Disintegrin and cysteine- rich domain | ||||||
Components | ADAM 10 | ||||||
Keywords | HYDROLASE / Extracellular / protease / Disintegrin | ||||||
Function / homology | Function and homology information Degradation of the extracellular matrix / ADAM10 endopeptidase / constitutive protein ectodomain proteolysis / regulation of vasculature development / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / epidermal growth factor receptor ligand maturation / monocyte activation / metalloendopeptidase activity involved in amyloid precursor protein catabolic process / protein catabolic process at postsynapse ...Degradation of the extracellular matrix / ADAM10 endopeptidase / constitutive protein ectodomain proteolysis / regulation of vasculature development / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / epidermal growth factor receptor ligand maturation / monocyte activation / metalloendopeptidase activity involved in amyloid precursor protein catabolic process / protein catabolic process at postsynapse / postsynapse organization / : / regulation of Notch signaling pathway / perinuclear endoplasmic reticulum / positive regulation of T cell chemotaxis / pore complex assembly / tetraspanin-enriched microdomain / metallodipeptidase activity / negative regulation of cell adhesion / adherens junction organization / regulation of postsynapse organization / Neutrophil degranulation / clathrin-coated vesicle / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / Golgi-associated vesicle / cochlea development / pore complex / amyloid precursor protein catabolic process / membrane protein ectodomain proteolysis / response to tumor necrosis factor / Notch signaling pathway / synaptic membrane / adherens junction / metalloendopeptidase activity / protein processing / SH3 domain binding / metallopeptidase activity / positive regulation of cell growth / endopeptidase activity / in utero embryonic development / postsynaptic density / axon / Golgi membrane / protein phosphorylation / negative regulation of gene expression / dendrite / glutamatergic synapse / positive regulation of cell population proliferation / protein kinase binding / Golgi apparatus / cell surface / protein homodimerization activity / metal ion binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.9 Å | ||||||
Authors | Janes, P.W. / Saha, N. / Barton, W.A. / Kolev, M.V. / Wimmer-Kleikamp, S.H. / Nievergall, E. / Blobel, C.P. / Himanen, J.-P. / Lackmann, M. / Nikolov, D.B. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2005 Title: Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Authors: Janes, P.W. / Saha, N. / Barton, W.A. / Kolev, M.V. / Wimmer-Kleikamp, S.H. / Nievergall, E. / Blobel, C.P. / Himanen, J.-P. / Lackmann, M. / Nikolov, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ao7.cif.gz | 37.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ao7.ent.gz | 29.8 KB | Display | PDB format |
PDBx/mmJSON format | 2ao7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ao/2ao7 ftp://data.pdbj.org/pub/pdb/validation_reports/ao/2ao7 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-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: 20870.668 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: ADAM10, MADM / Cell line (production host): HEK 293 / Production host: Homo sapiens (human) / References: UniProt: Q10741, ADAM10 endopeptidase |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 61.01 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 10 mM Hepes, 150 mM NaCl, 0.2M Ammonium Sulfate, 30% PEG 4000, soaked in 1 mM AuCl and 20% glycerol (cryoprotectant) , pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F2 / Wavelength: 1.034, 0.9789, 1.016 | ||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 1, 2004 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.9→8 Å / Num. obs: 11118 / % possible obs: 99.5 % / Redundancy: 12.4 % / Rmerge(I) obs: 0.066 / Net I/σ(I): 21.4 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.9→8 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.9→8 Å
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