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- PDB-1qad: Crystal Structure of the C-Terminal SH2 Domain of the P85 alpha R... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qad | ||||||
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Title | Crystal Structure of the C-Terminal SH2 Domain of the P85 alpha Regulatory Subunit of Phosphoinositide 3-Kinase: An SH2 domain mimicking its own substrate | ||||||
![]() | PI3-KINASE P85 ALPHA SUBUNIT | ||||||
![]() | TRANSFERASE / PHOPHOTYROSINE-BINDING DOMAIN / SUBSTRATE MIMICKING | ||||||
Function / homology | ![]() Signaling by ALK / MET activates PI3K/AKT signaling / RHOC GTPase cycle / CDC42 GTPase cycle / RAC1 GTPase cycle / RAC2 GTPase cycle / RHOD GTPase cycle / RHOJ GTPase cycle / RAC3 GTPase cycle / FLT3 Signaling ...Signaling by ALK / MET activates PI3K/AKT signaling / RHOC GTPase cycle / CDC42 GTPase cycle / RAC1 GTPase cycle / RAC2 GTPase cycle / RHOD GTPase cycle / RHOJ GTPase cycle / RAC3 GTPase cycle / FLT3 Signaling / RND3 GTPase cycle / RND2 GTPase cycle / RND1 GTPase cycle / PI3K events in ERBB4 signaling / Interleukin-7 signaling / GAB1 signalosome / PI3K events in ERBB2 signaling / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / IRS-mediated signalling / GPVI-mediated activation cascade / Signaling by SCF-KIT / Downstream signal transduction / PI3K/AKT activation / Role of phospholipids in phagocytosis / Tie2 Signaling / Role of LAT2/NTAL/LAB on calcium mobilization / Costimulation by the CD28 family / CD28 dependent PI3K/Akt signaling / RAF/MAP kinase cascade / Interleukin receptor SHC signaling / PI-3K cascade:FGFR1 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR4 / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / PI3K Cascade / PIP3 activates AKT signaling / GP1b-IX-V activation signalling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Synthesis of PIPs at the plasma membrane / RHOA GTPase cycle / RHOF GTPase cycle / DAP12 signaling / RHOU GTPase cycle / RHOV GTPase cycle / Regulation of signaling by CBL / Downstream TCR signaling / RHOG GTPase cycle / RET signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / VEGFA-VEGFR2 Pathway / phosphatidylinositol 3-kinase regulator activity / phosphatidylinositol 3-kinase activator activity / 1-phosphatidylinositol-3-kinase regulator activity / ErbB-3 class receptor binding / transmembrane receptor protein tyrosine kinase adaptor activity / positive regulation of endoplasmic reticulum unfolded protein response / enzyme-substrate adaptor activity / phosphatidylinositol 3-kinase complex, class IA / phosphatidylinositol 3-kinase complex / Extra-nuclear estrogen signaling / G alpha (q) signalling events / intracellular glucose homeostasis / phosphatidylinositol phosphate biosynthetic process / insulin receptor substrate binding / phosphatidylinositol 3-kinase binding / response to endoplasmic reticulum stress / phosphatidylinositol 3-kinase/protein kinase B signal transduction / substrate adhesion-dependent cell spreading / positive regulation of RNA splicing / insulin-like growth factor receptor signaling pathway / positive regulation of glucose import / positive regulation of protein localization to plasma membrane / insulin-like growth factor receptor binding / insulin receptor binding / positive regulation of protein import into nucleus / cellular response to insulin stimulus / protein transport / insulin receptor signaling pathway / protein stabilization / negative regulation of apoptotic process / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hoedemaeker, P.J. / Siegal, G. / Roe, M. / Driscoll, P.C. / Abrahams, J.P.A. | ||||||
![]() | ![]() Title: Crystal structure of the C-terminal SH2 domain of the p85alpha regulatory subunit of phosphoinositide 3-kinase: an SH2 domain mimicking its own substrate. Authors: Hoedemaeker, F.J. / Siegal, G. / Roe, S.M. / Driscoll, P.C. / Abrahams, J.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 60.8 KB | Display | ![]() |
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PDB format | ![]() | 44.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 413.5 KB | Display | ![]() |
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Full document | ![]() | 413.5 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 11.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bfjS S: Starting model for refinement |
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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
#1: Protein | Mass: 12615.052 Da / Num. of mol.: 1 / Fragment: C-TERMINAL SH2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.427 Å3/Da / Density % sol: 49.3 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: spontaneous crystallisation / pH: 7.5 Details: TRIS-HCL, NACL, EDTA, DTT, pH 7.5, SPONTANEOUS CRYSTALLISATION, temperature 277.0K | |||||||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Eck, M.J., (1993) Nature, 362, 87. / pH: 4.6 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 5, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→23.44 Å / Num. all: 10947 / Num. obs: 10947 / % possible obs: 98.7 % / Redundancy: 3.4 % / Biso Wilson estimate: 18 Å2 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 1.8→1.85 Å / Redundancy: 3 % / Mean I/σ(I) obs: 10.2 / % possible all: 84.5 |
Reflection | *PLUS Num. measured all: 37237 / Rmerge(I) obs: 0.044 |
Reflection shell | *PLUS % possible obs: 84.5 % / Num. unique obs: 677 / Num. measured obs: 2058 / Rmerge(I) obs: 0.068 |
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Processing
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Refinement | Starting model: 1BFJ Resolution: 1.8→23.44 Å / SU B: 2.3668 / SU ML: 0.07628 / Cross valid method: Rfree / ESU R Free: 0.14209 / Stereochemistry target values: ENGH & HUBER Details: CONJUGATED DIRECTION METHOD WITH MAXIMUM LIKELYHOOD TARGET (REFMAC_aniso)
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Refinement step | Cycle: LAST / Resolution: 1.8→23.44 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.158 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.85 Å / Rfactor Rfree: 0.231 / Num. reflection Rfree: 135 / Num. reflection Rwork: 1159 / Rfactor obs: 0.118 |