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Yorodumi- PDB-2x6m: Structure of a single domain camelid antibody fragment in complex... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2x6m | ||||||
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Title | Structure of a single domain camelid antibody fragment in complex with a C-terminal peptide of alpha-synuclein | ||||||
Components |
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Keywords | IMMUNE SYSTEM / PARKINSON'S DISEASE / ALZHEIMER DISEASE AMYLOID / NANOBODY / AFFINITY TAG | ||||||
Function / homology | Function and homology information negative regulation of mitochondrial electron transport, NADH to ubiquinone / neutral lipid metabolic process / regulation of phospholipase activity / negative regulation of monooxygenase activity / regulation of acyl-CoA biosynthetic process / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of norepinephrine uptake / positive regulation of glutathione peroxidase activity / positive regulation of SNARE complex assembly / positive regulation of hydrogen peroxide catabolic process ...negative regulation of mitochondrial electron transport, NADH to ubiquinone / neutral lipid metabolic process / regulation of phospholipase activity / negative regulation of monooxygenase activity / regulation of acyl-CoA biosynthetic process / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of norepinephrine uptake / positive regulation of glutathione peroxidase activity / positive regulation of SNARE complex assembly / positive regulation of hydrogen peroxide catabolic process / supramolecular fiber / negative regulation of transporter activity / mitochondrial membrane organization / negative regulation of chaperone-mediated autophagy / regulation of reactive oxygen species biosynthetic process / positive regulation of protein localization to cell periphery / regulation of synaptic vesicle recycling / negative regulation of platelet-derived growth factor receptor signaling pathway / negative regulation of exocytosis / regulation of glutamate secretion / regulation of norepinephrine uptake / response to iron(II) ion / SNARE complex assembly / positive regulation of neurotransmitter secretion / dopamine biosynthetic process / regulation of locomotion / positive regulation of inositol phosphate biosynthetic process / synaptic vesicle priming / regulation of macrophage activation / negative regulation of microtubule polymerization / dopamine uptake involved in synaptic transmission / synaptic vesicle transport / dynein complex binding / positive regulation of receptor recycling / regulation of dopamine secretion / protein kinase inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / response to type II interferon / cuprous ion binding / positive regulation of exocytosis / synaptic vesicle exocytosis / kinesin binding / positive regulation of endocytosis / mitochondrial ATP synthesis coupled electron transport / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / response to magnesium ion / regulation of presynapse assembly / synaptic vesicle endocytosis / negative regulation of serotonin uptake / alpha-tubulin binding / localization / phospholipid metabolic process / supramolecular fiber organization / axon terminus / inclusion body / cellular response to copper ion / cellular response to epinephrine stimulus / Hsp70 protein binding / excitatory postsynaptic potential / response to interleukin-1 / adult locomotory behavior / SNARE binding / positive regulation of release of sequestered calcium ion into cytosol / fatty acid metabolic process / long-term synaptic potentiation / phosphoprotein binding / protein tetramerization / regulation of transmembrane transporter activity / synapse organization / regulation of long-term neuronal synaptic plasticity / microglial cell activation / negative regulation of protein kinase activity / protein destabilization / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / ferrous iron binding / tau protein binding / PKR-mediated signaling / positive regulation of protein serine/threonine kinase activity / receptor internalization / phospholipid binding / synaptic vesicle membrane / positive regulation of inflammatory response / activation of cysteine-type endopeptidase activity involved in apoptotic process / actin cytoskeleton / positive regulation of peptidyl-serine phosphorylation / actin binding / cell cortex / histone binding / cellular response to oxidative stress / growth cone / postsynapse / chemical synaptic transmission / neuron apoptotic process / negative regulation of neuron apoptotic process / amyloid fibril formation / response to lipopolysaccharide / molecular adaptor activity / oxidoreductase activity / lysosome / transcription cis-regulatory region binding Similarity search - Function | ||||||
Biological species | CAMELUS DROMEDARIUS (Arabian camel) HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.62 Å | ||||||
Authors | DeGenst, E. / Guilliams, T. / Wellens, J. / O'Day, E.M. / Waudby, C.A. / Meehan, S. / Dumoulin, M. / Hsu, S.-T.D. / Cremades, N. / Verschueren, K.H.G. ...DeGenst, E. / Guilliams, T. / Wellens, J. / O'Day, E.M. / Waudby, C.A. / Meehan, S. / Dumoulin, M. / Hsu, S.-T.D. / Cremades, N. / Verschueren, K.H.G. / Pardon, E. / Wyns, L. / Steyaert, J. / Christodoulou, J. / Dobson, C.M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2010 Title: Structure and Properties of a Complex of Alpha-Synuclein and a Single-Domain Camelid Antibody. Authors: De Genst, E.J. / Guilliams, T. / Wellens, J. / O'Day, E.M. / Waudby, C.A. / Meehan, S. / Dumoulin, M. / Hsu, S.-T.D. / Cremades, N. / Verschueren, K.H.G. / Pardon, E. / Wyns, L. / Steyaert, ...Authors: De Genst, E.J. / Guilliams, T. / Wellens, J. / O'Day, E.M. / Waudby, C.A. / Meehan, S. / Dumoulin, M. / Hsu, S.-T.D. / Cremades, N. / Verschueren, K.H.G. / Pardon, E. / Wyns, L. / Steyaert, J. / Christodoulou, J. / Dobson, C.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2x6m.cif.gz | 44.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2x6m.ent.gz | 30.7 KB | Display | PDB format |
PDBx/mmJSON format | 2x6m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2x6m_validation.pdf.gz | 426.9 KB | Display | wwPDB validaton report |
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Full document | 2x6m_full_validation.pdf.gz | 427.1 KB | Display | |
Data in XML | 2x6m_validation.xml.gz | 9.7 KB | Display | |
Data in CIF | 2x6m_validation.cif.gz | 14 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x6/2x6m ftp://data.pdbj.org/pub/pdb/validation_reports/x6/2x6m | HTTPS FTP |
-Related structure data
Related structure data | 1hcvS S: Starting model for refinement |
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Similar structure data |
-Links
-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: Antibody | Mass: 13437.815 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: ENGINEERED FROM IMMUNISED DROMEDARY / Source: (gene. exp.) CAMELUS DROMEDARIUS (Arabian camel) / Tissue: BLOOD / Cell: LYMPHOCYTE / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): WK6 |
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#2: Protein/peptide | Mass: 1071.052 Da / Num. of mol.: 1 Fragment: C-TERMINAL FRAGMENT OF ALPHA-SYNUCLEIN, RESIDUES 132-140 Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P37840 |
#3: 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: 2.01 Å3/Da / Density % sol: 38.84 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 25% PEG6000, 100 MM HEPES PH 7.5, 100 MM LICL |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.815 |
Detector | Type: MAR555 FLAT PANEL / Detector: IMAGE PLATE |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.815 Å / Relative weight: 1 |
Reflection | Resolution: 1.62→30 Å / Num. obs: 15482 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 14.3 % / Biso Wilson estimate: 18.126 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 23.3 |
Reflection shell | Resolution: 1.62→1.71 Å / Redundancy: 14.2 % / Rmerge(I) obs: 0.54 / Mean I/σ(I) obs: 4.3 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1HCV Resolution: 1.62→43.56 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.95 / SU B: 3.577 / SU ML: 0.056 / Cross valid method: THROUGHOUT / ESU R: 0.094 / ESU R Free: 0.099 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.U VALUES RESIDUAL ONLY. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS.ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.91 Å2
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Refinement step | Cycle: LAST / Resolution: 1.62→43.56 Å
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Refine LS restraints |
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