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- PDB-2a5u: Crystal Structure of human PI3Kgamma complexed with AS605240 -

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Basic information

Entry
Database: PDB / ID: 2a5u
TitleCrystal Structure of human PI3Kgamma complexed with AS605240
ComponentsPhosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, gamma isoform
KeywordsTRANSFERASE / Protein-inhibitor complex / PI3Kg
Function / homology
Function and homology information


negative regulation of triglyceride catabolic process / secretory granule localization / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / regulation of calcium ion transmembrane transport / T cell chemotaxis ...negative regulation of triglyceride catabolic process / secretory granule localization / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / regulation of calcium ion transmembrane transport / T cell chemotaxis / negative regulation of fibroblast apoptotic process / phosphatidylinositol 3-kinase complex, class IB / sphingosine-1-phosphate receptor signaling pathway / phosphatidylinositol 3-kinase complex, class IA / dendritic cell chemotaxis / 1-phosphatidylinositol-4-phosphate 3-kinase activity / 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity / phosphatidylinositol-4,5-bisphosphate 3-kinase / phosphatidylinositol 3-kinase / phosphatidylinositol-3-phosphate biosynthetic process / 1-phosphatidylinositol-3-kinase activity / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / mast cell degranulation / hepatocyte apoptotic process / positive regulation of Rac protein signal transduction / regulation of cell adhesion mediated by integrin / Synthesis of PIPs at the plasma membrane / phosphatidylinositol-mediated signaling / phosphatidylinositol phosphate biosynthetic process / regulation of angiogenesis / phosphorylation / T cell proliferation / cellular response to cAMP / GPVI-mediated activation cascade / ephrin receptor binding / neutrophil chemotaxis / phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of endothelial cell migration / T cell activation / positive regulation of cytokine production / positive regulation of MAP kinase activity / platelet aggregation / endocytosis / G beta:gamma signalling through PI3Kgamma / kinase activity / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cytosolic calcium ion concentration / angiogenesis / adaptive immune response / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / non-specific serine/threonine protein kinase / protein kinase activity / inflammatory response / immune response / G protein-coupled receptor signaling pathway / innate immune response / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / identical protein binding / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
PIK3 catalytic subunit gamma, adaptor-binding domain / PIK3 catalytic subunit gamma adaptor-binding domain / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase, accessory domain (PIK) / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 / C2 domain / Phosphatidylinositol 3-kinase, adaptor-binding domain / Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile. ...PIK3 catalytic subunit gamma, adaptor-binding domain / PIK3 catalytic subunit gamma adaptor-binding domain / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase, accessory domain (PIK) / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 / C2 domain / Phosphatidylinositol 3-kinase, adaptor-binding domain / Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile. / PI3-kinase family, Ras-binding domain / Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain / PI3-kinase family, ras-binding domain / Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain profile. / C2 phosphatidylinositol 3-kinase-type domain / Phosphoinositide 3-kinase C2 / C2 phosphatidylinositol 3-kinase (PI3K)-type domain profile. / Phosphoinositide 3-kinase, region postulated to contain C2 domain / Phosphoinositide 3-kinase family, accessory domain (PIK domain) / Phosphoinositide 3-kinase family, accessory domain (PIK domain) / Phosphoinositide 3-kinase, accessory (PIK) domain superfamily / Phosphoinositide 3-kinase, accessory (PIK) domain / Phosphatidylinositol kinase / PIK helical domain profile. / Phosphatidylinositol 3- and 4-kinases signature 1. / Phosphatidylinositol 3- and 4-kinases signature 2. / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / C2 domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Ubiquitin-like (UB roll) / Alpha Horseshoe / Armadillo-type fold / Ubiquitin-like domain superfamily / Roll / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-QYT / Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsCamps, M. / Ruckle, T. / Ji, H. / Ardissone, V. / Rintelen, F. / Shaw, J. / Ferrandi, C. / Chabert, C. / Gillieron, C. / Francon, B. ...Camps, M. / Ruckle, T. / Ji, H. / Ardissone, V. / Rintelen, F. / Shaw, J. / Ferrandi, C. / Chabert, C. / Gillieron, C. / Francon, B. / Martin, T. / Gretener, D. / Perrin, D. / Leroy, D. / Vitte, P.-A. / Hirsch, E. / Wymann, M.P. / Cirillo, R. / Schwarz, M.K. / Rommel, C.
CitationJournal: NAT.MED. (N.Y.) / Year: 2005
Title: Blockade of PI3Kgamma suppresses joint inflammation and damage in mouse models of rheumatoid arthritis
Authors: Camps, M. / Ruckle, T. / Ji, H. / Ardissone, V. / Rintelen, F. / Shaw, J. / Ferrandi, C. / Chabert, C. / Gillieron, C. / Francon, B. / Martin, T. / Gretener, D. / Perrin, D. / Leroy, D. / ...Authors: Camps, M. / Ruckle, T. / Ji, H. / Ardissone, V. / Rintelen, F. / Shaw, J. / Ferrandi, C. / Chabert, C. / Gillieron, C. / Francon, B. / Martin, T. / Gretener, D. / Perrin, D. / Leroy, D. / Vitte, P.-A. / Hirsch, E. / Wymann, M.P. / Cirillo, R. / Schwarz, M.K. / Rommel, C.
History
DepositionJul 1, 2005Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Sep 20, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software / Item: _software.classification
Revision 1.4Oct 25, 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_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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-4,5-bisphosphate 3-kinase catalytic subunit, gamma isoform
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,0132
Polymers110,7561
Non-polymers2571
Water36020
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)140.446, 67.406, 105.971
Angle α, β, γ (deg.)90.00, 96.35, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, gamma isoform / phosphatidylinositol 3-kinase catalytic subunit / PI3-kinase p110 subunit gamma / PtdIns- 3-kinase ...phosphatidylinositol 3-kinase catalytic subunit / PI3-kinase p110 subunit gamma / PtdIns- 3-kinase p110 / PI3K / PI3Kgamma


Mass: 110756.164 Da / Num. of mol.: 1 / Fragment: P110 SUBUNIT GAMMA, residues 143-1101
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line: SF9 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P48736, phosphatidylinositol-4,5-bisphosphate 3-kinase
#2: Chemical ChemComp-QYT / (5E)-5-(QUINOXALIN-6-YLMETHYLENE)-1,3-THIAZOLIDINE-2,4-DIONE / 5-QUINOXALIN-6-YLMETHYLENE-THIAZOLIDINE-2,4-DIONE


Mass: 257.268 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C12H7N3O2S
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O

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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: 2.61 Å3/Da / Density % sol: 53 %
Crystal growTemperature: 300 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 22% PEG 4K, 100mM Tris-HCl, 200mM (NH4)2SO4, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 300K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.0716 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: May 5, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0716 Å / Relative weight: 1
ReflectionResolution: 2.7→105.41 Å / Num. all: 31524 / Num. obs: 28933 / % possible obs: 96.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Rmerge(I) obs: 0.072 / Rsym value: 0.072 / Net I/σ(I): 7
Reflection shellResolution: 2.7→2.85 Å / % possible obs: 98.5 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.266 / Mean I/σ(I) obs: 2.3 / Num. measured obs: 3893 / Num. unique all: 3893 / Rsym value: 0.266 / % possible all: 98.5

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Processing

Software
NameVersionClassificationNB
SCALAdata scaling
CNSrefinement
PDB_EXTRACT1.7data extraction
MOSFLMdata reduction
CCP4(SCALA)data scaling
AMoREphasing
CNX2002refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1e8y

1e8y


Resolution: 2.7→19.58 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1306742.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflectionSelection details
Rfree0.351 2591 9.8 %RANDOM
Rwork0.279 ---
all0.285 26342 --
obs0.285 26342 96.6 %-
Solvent computationSolvent model: BABINET / Bsol: 280 Å2
Displacement parametersBiso mean: 62 Å2
Baniso -1Baniso -2Baniso -3
1--10.3 Å20 Å26.6 Å2
2--8.04 Å20 Å2
3---2.27 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.59 Å0.41 Å
Luzzati d res low-5 Å
Luzzati sigma a0.58 Å0.3 Å
Refinement stepCycle: LAST / Resolution: 2.7→19.58 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6806 0 18 20 6844
Refine LS restraints
Refine-IDTypeDev idealWeight
X-RAY DIFFRACTIONc_bond_d0.007
X-RAY DIFFRACTIONc_angle_deg1.2
X-RAY DIFFRACTIONc_dihedral_angle_d21.8
X-RAY DIFFRACTIONc_improper_angle_d0.81
X-RAY DIFFRACTIONc_mcbond_it4.11.5
X-RAY DIFFRACTIONc_mcangle_it6.162
X-RAY DIFFRACTIONc_scbond_it5.862
X-RAY DIFFRACTIONc_scangle_it7.912.5
Refine LS restraints NCSNCS model details: RESTRAINTS
LS refinement shellResolution: 2.7→2.87 Å / Rfactor Rfree error: 0.025 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.497 410 9.2 %
Rwork0.371 4043 -
all-4453 -
obs--98.6 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2water_rep.paramwater.top
X-RAY DIFFRACTION3ion.paramion.top
X-RAY DIFFRACTION4inh.paraminh.top

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