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- PDB-3i5s: Crystal structure of PI3K SH3 -

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Basic information

Entry
Database: PDB / ID: 3i5s
TitleCrystal structure of PI3K SH3
ComponentsPhosphatidylinositol 3-kinase regulatory subunit alpha
KeywordsPROTEIN BINDING / SH3 domain / Alternative splicing / Disease mutation / Host-virus interaction / Phosphoprotein / Polymorphism / SH2 domain / Ubl conjugation
Function / homology
Function and homology information


perinuclear endoplasmic reticulum membrane / regulation of toll-like receptor 4 signaling pathway / phosphatidylinositol kinase activity / phosphatidylinositol 3-kinase regulator activity / 1-phosphatidylinositol-3-kinase regulator activity / positive regulation of endoplasmic reticulum unfolded protein response / phosphatidylinositol 3-kinase activator activity / T follicular helper cell differentiation / IRS-mediated signalling / interleukin-18-mediated signaling pathway ...perinuclear endoplasmic reticulum membrane / regulation of toll-like receptor 4 signaling pathway / phosphatidylinositol kinase activity / phosphatidylinositol 3-kinase regulator activity / 1-phosphatidylinositol-3-kinase regulator activity / positive regulation of endoplasmic reticulum unfolded protein response / phosphatidylinositol 3-kinase activator activity / T follicular helper cell differentiation / IRS-mediated signalling / interleukin-18-mediated signaling pathway / phosphatidylinositol 3-kinase regulatory subunit binding / myeloid leukocyte migration / PI3K events in ERBB4 signaling / neurotrophin TRKA receptor binding / positive regulation of focal adhesion disassembly / cis-Golgi network / Activated NTRK2 signals through PI3K / ErbB-3 class receptor binding / transmembrane receptor protein tyrosine kinase adaptor activity / negative regulation of stress fiber assembly / Activated NTRK3 signals through PI3K / phosphatidylinositol 3-kinase complex / Co-stimulation by ICOS / RHOD GTPase cycle / Signaling by cytosolic FGFR1 fusion mutants / Nephrin family interactions / RHOF GTPase cycle / kinase activator activity / Signaling by LTK in cancer / Signaling by LTK / RND1 GTPase cycle / positive regulation of leukocyte migration / RND2 GTPase cycle / RND3 GTPase cycle / positive regulation of filopodium assembly / phosphatidylinositol 3-kinase complex, class IA / MET activates PI3K/AKT signaling / PI3K/AKT activation / growth hormone receptor signaling pathway / insulin binding / Signaling by ALK / RHOV GTPase cycle / RHOB GTPase cycle / natural killer cell mediated cytotoxicity / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / GP1b-IX-V activation signalling / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / RHOC GTPase cycle / RHOJ GTPase cycle / negative regulation of osteoclast differentiation / phosphatidylinositol phosphate biosynthetic process / Synthesis of PIPs at the plasma membrane / RHOU GTPase cycle / CDC42 GTPase cycle / RET signaling / T cell differentiation / Interleukin-3, Interleukin-5 and GM-CSF signaling / insulin receptor substrate binding / PI3K events in ERBB2 signaling / RHOG GTPase cycle / negative regulation of cell-matrix adhesion / PI3K Cascade / extrinsic apoptotic signaling pathway via death domain receptors / Role of LAT2/NTAL/LAB on calcium mobilization / RHOA GTPase cycle / CD28 dependent PI3K/Akt signaling / RAC3 GTPase cycle / RAC2 GTPase cycle / Interleukin receptor SHC signaling / Role of phospholipids in phagocytosis / enzyme-substrate adaptor activity / GAB1 signalosome / phosphatidylinositol 3-kinase binding / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / GPVI-mediated activation cascade / positive regulation of lamellipodium assembly / Signaling by FGFR4 in disease / insulin-like growth factor receptor binding / Signaling by FLT3 ITD and TKD mutants / phosphotyrosine residue binding / Signaling by FGFR3 in disease / Tie2 Signaling / RAC1 GTPase cycle / Signaling by FGFR2 in disease / Signaling by FLT3 fusion proteins / FLT3 Signaling / substrate adhesion-dependent cell spreading / Signaling by FGFR1 in disease / insulin-like growth factor receptor signaling pathway / Downstream signal transduction / positive regulation of smooth muscle cell proliferation / osteoclast differentiation / Interleukin-7 signaling / B cell differentiation / intracellular glucose homeostasis / response to endoplasmic reticulum stress
Similarity search - Function
Phosphatidylinositol 3-kinase regulatory subunit alpha, SH3 domain / PIK3R1, inter-SH2 domain / PI3K p85 subunit, C-terminal SH2 domain / PI3K regulatory subunit p85-related , inter-SH2 domain / PI3K p85 subunit, N-terminal SH2 domain / Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases ...Phosphatidylinositol 3-kinase regulatory subunit alpha, SH3 domain / PIK3R1, inter-SH2 domain / PI3K p85 subunit, C-terminal SH2 domain / PI3K regulatory subunit p85-related , inter-SH2 domain / PI3K p85 subunit, N-terminal SH2 domain / Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / Rho GTPase activation protein / SH3 Domains / SH2 domain / Src homology 2 (SH2) domain profile. / SH3 type barrels. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Roll / Mainly Beta
Similarity search - Domain/homology
Phosphatidylinositol 3-kinase regulatory subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsBatra-Safferling, R. / Granzin, J. / Modder, S. / Hoffmann, S. / Willbold, D.
CitationJournal: Biol.Chem. / Year: 2010
Title: Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding.
Authors: Batra-Safferling, R. / Granzin, J. / Modder, S. / Hoffmann, S. / Willbold, D.
History
DepositionJul 6, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 2, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Phosphatidylinositol 3-kinase regulatory subunit alpha
B: Phosphatidylinositol 3-kinase regulatory subunit alpha
C: Phosphatidylinositol 3-kinase regulatory subunit alpha
D: Phosphatidylinositol 3-kinase regulatory subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,8415
Polymers37,7454
Non-polymers961
Water00
1
A: Phosphatidylinositol 3-kinase regulatory subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,5322
Polymers9,4361
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Phosphatidylinositol 3-kinase regulatory subunit alpha


Theoretical massNumber of molelcules
Total (without water)9,4361
Polymers9,4361
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Phosphatidylinositol 3-kinase regulatory subunit alpha


Theoretical massNumber of molelcules
Total (without water)9,4361
Polymers9,4361
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Phosphatidylinositol 3-kinase regulatory subunit alpha


Theoretical massNumber of molelcules
Total (without water)9,4361
Polymers9,4361
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)49.333, 61.049, 61.014
Angle α, β, γ (deg.)90.00, 111.38, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
11A
21B
31C
41D

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: LYS / End label comp-ID: LYS / Auth seq-ID: 5 - 80 / Label seq-ID: 5 - 80

Dom-IDSelection detailsAuth asym-IDLabel asym-ID
1chain A and (resseq 5:80 )AA
2chain B and (resseq 5:80 )BB
3chain C and (resseq 5:80 )CC
4chain D and (resseq 5:80 )DD

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Components

#1: Protein
Phosphatidylinositol 3-kinase regulatory subunit alpha / PI3-kinase p85 subunit alpha / PtdIns-3-kinase p85-alpha / PI3K


Mass: 9436.354 Da / Num. of mol.: 4 / Fragment: SH3 domain (UNP residues 1-83)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GRB1, PIK3R1 / Plasmid: pGEX / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P27986
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.27 Å3/Da / Density % sol: 45.73 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 5.5
Details: 100mM Na-citrate, 0.5M ammonium sulfate, 1M lithium sulfate, pH 5.5, VAPOR DIFFUSION, temperature 293.0K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 3, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 3→45.94 Å / Num. all: 6884 / Num. obs: 6390 / % possible obs: 94 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 54.05 Å2 / Rmerge(I) obs: 0.113 / Rsym value: 0.113 / Net I/σ(I): 10.3

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
MOLREPphasing
PHENIX(phenix.refine)refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1pht

1pht


Resolution: 3→45.938 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.6 / σ(F): 0.04 / Phase error: 31.47 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.299 280 4.56 %
Rwork0.24 5856 -
obs0.243 6136 89.15 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 47.941 Å2 / ksol: 0.388 e/Å3
Displacement parametersBiso max: 134.61 Å2 / Biso mean: 35.05 Å2 / Biso min: 10.43 Å2
Baniso -1Baniso -2Baniso -3
1-9.342 Å2-0 Å2-1.278 Å2
2---5.083 Å20 Å2
3----4.258 Å2
Refinement stepCycle: LAST / Resolution: 3→45.938 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2484 0 5 0 2489
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0052540
X-RAY DIFFRACTIONf_angle_d0.7993426
X-RAY DIFFRACTIONf_dihedral_angle_d17.75912
X-RAY DIFFRACTIONf_chiral_restr0.056336
X-RAY DIFFRACTIONf_plane_restr0.003460
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A610X-RAY DIFFRACTIONPOSITIONAL0.024
12B610X-RAY DIFFRACTIONPOSITIONAL0.024
13C614X-RAY DIFFRACTIONPOSITIONAL0.021
14D610X-RAY DIFFRACTIONPOSITIONAL0.023
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0002-3.77960.37471490.28742846X-RAY DIFFRACTION88
3.7796-45.94350.23871310.20863010X-RAY DIFFRACTION91

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