+Open data
-Basic information
Entry | Database: PDB / ID: 1by1 | ||||||
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Title | DBL homology domain from beta-PIX | ||||||
Components | PROTEIN (PIX) | ||||||
Keywords | TRANSPORT PROTEIN / RHO-GTPASE EXCHANGE FACTOR | ||||||
Function / homology | Function and homology information negative regulation of microtubule nucleation / positive regulation of lamellipodium morphogenesis / focal adhesion assembly / gamma-tubulin binding / positive regulation of fibroblast migration / Ephrin signaling / lamellipodium assembly / RHOV GTPase cycle / Activation of RAC1 downstream of NMDARs / NRAGE signals death through JNK ...negative regulation of microtubule nucleation / positive regulation of lamellipodium morphogenesis / focal adhesion assembly / gamma-tubulin binding / positive regulation of fibroblast migration / Ephrin signaling / lamellipodium assembly / RHOV GTPase cycle / Activation of RAC1 downstream of NMDARs / NRAGE signals death through JNK / mitotic spindle pole / RHOJ GTPase cycle / Golgi organization / RHOQ GTPase cycle / CDC42 GTPase cycle / RHOU GTPase cycle / Rho protein signal transduction / RHOA GTPase cycle / ephrin receptor signaling pathway / positive regulation of substrate adhesion-dependent cell spreading / ruffle / RAC1 GTPase cycle / guanyl-nucleotide exchange factor activity / EGFR downregulation / positive regulation of GTPase activity / G alpha (12/13) signalling events / lamellipodium / nervous system development / cell cortex / postsynapse / neuron projection / positive regulation of apoptotic process / focal adhesion / centrosome / neuronal cell body / protein kinase binding / signal transduction / protein-containing complex / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, TORSION ANGLE DYNAMICS | ||||||
Authors | Aghazadeh, B. / Zhu, K. / Kubiseski, T.J. / Liu, G.A. / Pawson, T. / Zheng, Y. / Rosen, M.K. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1998 Title: Structure and Mutagenesis of the Dbl Homology Domain Authors: Aghazadeh, B. / Zhu, K. / Kubiseski, T.J. / Liu, G.A. / Pawson, T. / Zheng, Y. / Rosen, M.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1by1.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1by1.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 1by1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/by/1by1 ftp://data.pdbj.org/pub/pdb/validation_reports/by/1by1 | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 23972.473 Da / Num. of mol.: 1 / Fragment: DBL HOMOLOGY DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET11A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q14155 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING A COMBINATION OF TRIPLE- AND QUADRUPLE- RESONANCE NMR EXPERIMENTS ON 13C/ 15N AND PARTIALLY OR FULLY DEUTERATED SAMPLES WITH SELECTIVE METHYL LABELING AT ...Text: THE STRUCTURE WAS DETERMINED USING A COMBINATION OF TRIPLE- AND QUADRUPLE- RESONANCE NMR EXPERIMENTS ON 13C/ 15N AND PARTIALLY OR FULLY DEUTERATED SAMPLES WITH SELECTIVE METHYL LABELING AT VALINE,LEUCINE AND ISOLEUCINES. |
-Sample preparation
Details | Contents: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 150mM / pH: 7.0 / Pressure: 1 atm / Temperature: 311 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITY INOVA / Manufacturer: Varian / Model: UNITY INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING, TORSION ANGLE DYNAMICS / Software ordinal: 1 Details: X-PLOR 3.851 WAS USED IN COMBINATION WITH ARIA (REF. M. NILGES) | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 80 / Conformers submitted total number: 20 |