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Open data
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Basic information
| Entry | Database: PDB / ID: 6qp8 | |||||||||
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| Title | Drosophila Semaphorin 2b | |||||||||
Components | IP13724p | |||||||||
Keywords | SIGNALING PROTEIN / axon guidance cue / developmental protein / cell signalling / semaphorin / signalling protein | |||||||||
| Function / homology | Function and homology informationsynaptic target attraction / olfactory bulb axon guidance / Sema3A PAK dependent Axon repulsion / : / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / dendrite guidance / Sema4D induced cell migration and growth-cone collapse / Other semaphorin interactions / semaphorin receptor binding / dendrite self-avoidance ...synaptic target attraction / olfactory bulb axon guidance / Sema3A PAK dependent Axon repulsion / : / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / dendrite guidance / Sema4D induced cell migration and growth-cone collapse / Other semaphorin interactions / semaphorin receptor binding / dendrite self-avoidance / regulation of cell-matrix adhesion / chemorepellent activity / negative chemotaxis / semaphorin-plexin signaling pathway / axon guidance / positive regulation of cell migration / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.33 Å | |||||||||
Authors | Robinson, R.A. / Rozbesky, D. / Harlos, K. / Siebold, C. / Jones, E.Y. | |||||||||
| Funding support | United Kingdom, 2items
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Citation | Journal: Nat Commun / Year: 2019Title: Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning. Authors: Rozbesky, D. / Robinson, R.A. / Jain, V. / Renner, M. / Malinauskas, T. / Harlos, K. / Siebold, C. / Jones, E.Y. | |||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6qp8.cif.gz | 540.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6qp8.ent.gz | 445.2 KB | Display | PDB format |
| PDBx/mmJSON format | 6qp8.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qp/6qp8 ftp://data.pdbj.org/pub/pdb/validation_reports/qp/6qp8 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 6fkkC ![]() 6qp7C ![]() 6qp9C ![]() 1olzS 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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| Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
| #1: Protein | Mass: 74920.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: Sema2b, CG30322, CG4383, Dmel\CG33960, Sema-2b, sema-2b, sema2b, SemaIIB, CG33960, Dmel_CG33960 Production host: Homo sapiens (human) / References: UniProt: Q29QV5, UniProt: A0A0B4KG38*PLUS |
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-Sugars , 9 types, 14 molecules 
| #2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose #3: Polysaccharide | alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-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: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #5: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #6: Polysaccharide | #7: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #8: Polysaccharide | alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #9: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | #10: Sugar | |
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-Non-polymers , 3 types, 714 molecules 




| #11: Chemical | | #12: Chemical | ChemComp-FLC / | #13: Water | ChemComp-HOH / | |
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-Details
| Has protein modification | 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: 4.23 Å3/Da / Density % sol: 70.93 % |
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| Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 5 / Details: 0.1 M trisodium citrate (pH 5.0), 10% PEG 6000 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1.27165 Å |
| Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 27, 2009 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.27165 Å / Relative weight: 1 |
| Reflection | Resolution: 2.33→65.667 Å / Num. obs: 101324 / % possible obs: 98.42 % / Redundancy: 7.6 % / Rmerge(I) obs: 0.182 / Net I/σ(I): 10.45 |
| Reflection shell | Resolution: 2.33→2.3565 Å |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1OLZ Resolution: 2.33→65.667 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 23.42
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.33→65.667 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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About Yorodumi





X-RAY DIFFRACTION
United Kingdom, 2items
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PDBj






Homo sapiens (human)
