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Yorodumi- PDB-5l5g: Plexin A2 full extracellular region, domains 1 to 8 modeled, data... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5l5g | ||||||
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Title | Plexin A2 full extracellular region, domains 1 to 8 modeled, data to 10 angstrom | ||||||
Components | Plexin-A2 | ||||||
Keywords | SIGNALING PROTEIN / receptor / signaling / axon guidance | ||||||
Function / homology | Function and homology information cerebellar granule cell precursor tangential migration / CRMPs in Sema3A signaling / Sema3A PAK dependent Axon repulsion / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / semaphorin-plexin signaling pathway involved in axon guidance / limb bud formation / semaphorin receptor complex / pharyngeal system development / semaphorin receptor activity / negative regulation of cell adhesion ...cerebellar granule cell precursor tangential migration / CRMPs in Sema3A signaling / Sema3A PAK dependent Axon repulsion / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / semaphorin-plexin signaling pathway involved in axon guidance / limb bud formation / semaphorin receptor complex / pharyngeal system development / semaphorin receptor activity / negative regulation of cell adhesion / neural tube development / centrosome localization / positive regulation of axonogenesis / semaphorin-plexin signaling pathway / somitogenesis / regulation of cell migration / regulation of cell shape / collagen-containing extracellular matrix / cell surface receptor signaling pathway / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 10 Å | ||||||
Authors | Janssen, B.J.C. / Kong, Y. / Malinauskas, T. / Vangoor, V.R. / Coles, C.H. / Kaufmann, R. / Ni, T. / Gilbert, R.J.C. / Padilla-Parra, S. / Pasterkamp, R.J. / Jones, E.Y. | ||||||
Citation | Journal: Neuron / Year: 2016 Title: Structural Basis for Plexin Activation and Regulation. Authors: Kong, Y. / Janssen, B.J. / Malinauskas, T. / Vangoor, V.R. / Coles, C.H. / Kaufmann, R. / Ni, T. / Gilbert, R.J. / Padilla-Parra, S. / Pasterkamp, R.J. / Jones, E.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5l5g.cif.gz | 654.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5l5g.ent.gz | 498.7 KB | Display | PDB format |
PDBx/mmJSON format | 5l5g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l5/5l5g ftp://data.pdbj.org/pub/pdb/validation_reports/l5/5l5g | HTTPS FTP |
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-Related structure data
Related structure data | 5l56C 5l59C 5l5cC 5l5kC 5l5lC 5l5mC 5l5nC 5l74C 5l7nC 3oktS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-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: 133579.266 Da / Num. of mol.: 4 / Fragment: UNP residues 33-1231 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Plxna2, Kiaa0463 / Cell line (production host): Hek293 / Production host: Homo sapiens (human) / References: UniProt: P70207 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density % sol: 85 % |
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Crystal grow | Temperature: 293.5 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.68 M potassium/sodium tartrate, 85 mM HEPES, pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97922 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 26, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97922 Å / Relative weight: 1 |
Reflection | Resolution: 10→63.055 Å / Num. obs: 11079 / % possible obs: 93.9 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.187 / Net I/σ(I): 5.1 |
Reflection shell | Highest resolution: 10 Å / Rmerge(I) obs: 0.882 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3OKT Resolution: 10→63.055 Å / SU ML: 1.75 / Cross valid method: FREE R-VALUE / σ(F): 0.69 / Phase error: 41.78 Details: THE AUTHORS STATE THAT DUE TO THE LOW RESOLUTION OF THE DIFFRACTION DATA THE STRUCTURE WAS ONLY SUBJECTED TO RIGID BODY REFINEMENT WITH EACH DOMAIN AS RIGID BODY. THE STRUCTURE IS BASED ON ...Details: THE AUTHORS STATE THAT DUE TO THE LOW RESOLUTION OF THE DIFFRACTION DATA THE STRUCTURE WAS ONLY SUBJECTED TO RIGID BODY REFINEMENT WITH EACH DOMAIN AS RIGID BODY. THE STRUCTURE IS BASED ON PDB ENTRIES 3OKT AND 5L56. THE AUTHORS HAVE NOT FURTHER REFINED THE RESULTING COORDINATES NOR CORRECTED RESULTING CLASHES BETWEEN ATOMS AND DEVIATING PEPTIDE LINKAGES BETWEEN DOMAINS.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 10→63.055 Å
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Refine LS restraints |
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LS refinement shell |
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