+Open data
-Basic information
Entry | Database: PDB / ID: 1u3o | ||||||
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Title | Solution structure of rat Kalirin N-terminal SH3 domain | ||||||
Components | Huntingtin-associated protein-interacting protein | ||||||
Keywords | SIGNALING PROTEIN / SH3 / cis-Proline | ||||||
Function / homology | Function and homology information RHOG GTPase cycle / NRAGE signals death through JNK / G alpha (12/13) signalling events / MAPK6/MAPK4 signaling / RAC1 GTPase cycle / maternal process involved in parturition / RHOA GTPase cycle / modification of postsynaptic actin cytoskeleton / regulation of dendrite development / negative regulation of growth hormone secretion ...RHOG GTPase cycle / NRAGE signals death through JNK / G alpha (12/13) signalling events / MAPK6/MAPK4 signaling / RAC1 GTPase cycle / maternal process involved in parturition / RHOA GTPase cycle / modification of postsynaptic actin cytoskeleton / regulation of dendrite development / negative regulation of growth hormone secretion / regulation of modification of postsynaptic actin cytoskeleton / positive regulation of dendritic spine morphogenesis / habituation / EPHB-mediated forward signaling / maternal behavior / G alpha (q) signalling events / NMDA selective glutamate receptor signaling pathway / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / neurotransmitter receptor localization to postsynaptic specialization membrane / neuromuscular junction development / extrinsic component of membrane / social behavior / lactation / adult locomotory behavior / axonogenesis / guanyl-nucleotide exchange factor activity / axon guidance / memory / presynapse / nervous system development / postsynaptic density / cytoskeleton / non-specific serine/threonine protein kinase / intracellular signal transduction / protein serine kinase activity / protein serine/threonine kinase activity / neuronal cell body / glutamatergic synapse / perinuclear region of cytoplasm / enzyme binding / ATP binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / Torsion angle dynamics, simulated annealing | ||||||
Authors | Schiller, M.R. / Chakrabarti, K. / King, G.F. / Schiller, N.I. / Eipper, B.A. / Maciejewski, M.W. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: Regulation of RhoGEF Activity by Intramolecular and Intermolecular SH3 Domain Interactions. Authors: Schiller, M.R. / Chakrabarti, K. / King, G.F. / Schiller, N.I. / Eipper, B.A. / Maciejewski, M.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1u3o.cif.gz | 387.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1u3o.ent.gz | 323.4 KB | Display | PDB format |
PDBx/mmJSON format | 1u3o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u3/1u3o ftp://data.pdbj.org/pub/pdb/validation_reports/u3/1u3o | 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: 8578.576 Da / Num. of mol.: 1 / Fragment: SH3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Kalirin, HAPIP, Duo / Organ: brain / Plasmid: pGEX6P / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P97924 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 200 mM / pH: 6.4 / Pressure: ambient / Temperature: 298 K |
-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: Torsion angle dynamics, simulated annealing / Software ordinal: 1 Details: The structure is based on a total of 1017 restraints, with 893 NOE-derived distance constraints, 102 dihedral angle restraints, and 22 hydrogen bond restraints. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |