+Open data
-Basic information
Entry | Database: PDB / ID: 7y4q | ||||||||||||
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Title | Semaphorin 6D in complex with Plexin A1 | ||||||||||||
Components |
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Keywords | SIGNALING PROTEIN / signaling complex | ||||||||||||
Function / homology | Function and homology information Other semaphorin interactions / olfactory nerve formation / dichotomous subdivision of terminal units involved in salivary gland branching / semaphorin receptor binding / gonadotrophin-releasing hormone neuronal migration to the hypothalamus / Other semaphorin interactions / semaphorin-plexin signaling pathway involved in axon guidance / negative regulation of smooth muscle cell migration / negative regulation of axon extension involved in axon guidance / ventricular system development ...Other semaphorin interactions / olfactory nerve formation / dichotomous subdivision of terminal units involved in salivary gland branching / semaphorin receptor binding / gonadotrophin-releasing hormone neuronal migration to the hypothalamus / Other semaphorin interactions / semaphorin-plexin signaling pathway involved in axon guidance / negative regulation of smooth muscle cell migration / negative regulation of axon extension involved in axon guidance / ventricular system development / semaphorin receptor complex / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / chemorepellent activity / semaphorin receptor activity / CRMPs in Sema3A signaling / negative regulation of cell adhesion / RHOD GTPase cycle / regulation of smooth muscle cell migration / RND1 GTPase cycle / neural crest cell migration / smooth muscle cell migration / neuron projection extension / negative chemotaxis / positive regulation of axonogenesis / regulation of GTPase activity / positive regulation of smooth muscle cell migration / semaphorin-plexin signaling pathway / Sema3A PAK dependent Axon repulsion / regulation of cell migration / axon guidance / regulation of cell shape / positive regulation of cell migration / Golgi apparatus / extracellular space / extracellular exosome / nucleoplasm / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) Rattus norvegicus (Norway rat) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.7 Å | ||||||||||||
Authors | Tanaka, T. / Neyazaki, M. / Nogi, T. | ||||||||||||
Funding support | Japan, 3items
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Citation | Journal: Protein Sci. / Year: 2022 Title: Hybrid in vitro/in silico analysis of low-affinity protein-protein interactions that regulate signal transduction by Sema6D. Authors: Tanaka, T. / Ekimoto, T. / Nagatomo, M. / Neyazaki, M. / Shimoji, E. / Yamane, T. / Kanagawa, S. / Oi, R. / Mihara, E. / Takagi, J. / Akashi, S. / Ikeguchi, M. / Nogi, T. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7y4q.cif.gz | 592.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7y4q.ent.gz | 390.2 KB | Display | PDB format |
PDBx/mmJSON format | 7y4q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y4/7y4q ftp://data.pdbj.org/pub/pdb/validation_reports/y4/7y4q | HTTPS FTP |
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-Related structure data
Related structure data | 7y4oC 7y4pC 7cyt 7d07 S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 77079.102 Da / Num. of mol.: 2 / Fragment: ectodomain fragment Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PLXNA1, NOV, PLXN1 / Cell line (production host): HEK293S GnT1- / Production host: Homo sapiens (human) / References: UniProt: Q9UIW2 #2: Protein | Mass: 62522.633 Da / Num. of mol.: 2 / Fragment: ectodomain fragment / Mutation: S332G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Sema6d / Cell line (production host): CHO-lec 3.2.8.1 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: A0A0G2JZC4 #3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #4: Sugar | ChemComp-NAG / Has ligand of interest | Y | |
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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 Matthews: 9.82 Å3/Da / Density % sol: 87.48 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 7.4 / Details: 150 mM NaCl and 10 mM Tris-Cl (pH 7.4) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 0.98 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 14, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 4.7→49.43 Å / Num. obs: 110174 / % possible obs: 99.2 % / Redundancy: 3.4 % / Biso Wilson estimate: 155.92 Å2 / Rmerge(I) obs: 0.17 / Net I/σ(I): 6.1 |
Reflection shell | Resolution: 4.7→4.84 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.938 / Mean I/σ(I) obs: 1.5 / Num. unique obs: 4580 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7D07, 7CYT Resolution: 4.7→49.43 Å / SU ML: 0.6709 / Cross valid method: FREE R-VALUE / σ(F): 0.05 / Phase error: 27.178 / Stereochemistry target values: GeoStd + Monomer Library
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 200.63 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4.7→49.43 Å
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Refine LS restraints |
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LS refinement shell |
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