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Open data
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Basic information
Entry | Database: PDB / ID: 1ipg | ||||||
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Title | SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P | ||||||
![]() | BEM1 PROTEIN | ||||||
![]() | SIGNALING PROTEIN / ubiquitin alpha/beta roll | ||||||
Function / homology | ![]() RHO GTPases Activate NADPH Oxidases / conjugation with cellular fusion / cell morphogenesis involved in conjugation with cellular fusion / PAR polarity complex / site of polarized growth / superoxide-generating NADPH oxidase activator activity / cellular bud site selection / incipient cellular bud site / cellular bud tip / maintenance of protein location ...RHO GTPases Activate NADPH Oxidases / conjugation with cellular fusion / cell morphogenesis involved in conjugation with cellular fusion / PAR polarity complex / site of polarized growth / superoxide-generating NADPH oxidase activator activity / cellular bud site selection / incipient cellular bud site / cellular bud tip / maintenance of protein location / cellular bud neck / mating projection tip / regulation of Rho protein signal transduction / phosphatidylinositol-3-phosphate binding / superoxide anion generation / protein-macromolecule adaptor activity / cell cortex / molecular adaptor activity / cytoskeleton / mitochondrion / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / dynamical simulated annealing | ||||||
![]() | Terasawa, H. / Noda, Y. / Ito, T. / Hatanaka, H. / Ichikawa, S. / Ogura, K. / Sumimoto, H. / Inagaki, F. | ||||||
![]() | ![]() Title: Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. Authors: Terasawa, H. / Noda, Y. / Ito, T. / Hatanaka, H. / Ichikawa, S. / Ogura, K. / Sumimoto, H. / Inagaki, F. #1: ![]() Title: Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions Authors: Ito, T. / Matsui, Y. / Ago, T. / Ota, K. / Sumimoto, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.1 KB | Display | ![]() |
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PDB format | ![]() | 26 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 243.7 KB | Display | ![]() |
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Full document | ![]() | 243.5 KB | Display | |
Data in XML | ![]() | 4.7 KB | Display | |
Data in CIF | ![]() | 5.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 9519.925 Da / Num. of mol.: 1 / Fragment: PB1 DOMAIN(RESIDUES 472-551) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PPROEX-HTA / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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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 triple-resonance NMR spectroscopy. |
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Sample preparation
Details | Contents: 2mM Bem PB1 U-15N, 13C; 50mM potassium phosphate pH 6.3; 150mM sodium chloride; 1mM sodium azide; 90% H2O, 10% D2O Solvent system: 90% H2O, 10% D2O or 100% D2O |
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Sample conditions | Ionic strength: 50mM potassium phosphate; 150mM sodium chloride pH: 6.3 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: dynamical simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1334 restraints, 1269 are NOE-derived distance constraints, 65 dihedral angle restraints. | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |