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- PDB-1jyq: Xray Structure of Grb2 SH2 Domain Complexed with a Highly Affine ... -

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Basic information

Entry
Database: PDB / ID: 1jyq
TitleXray Structure of Grb2 SH2 Domain Complexed with a Highly Affine Phospho Peptide
Components
  • GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
  • mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor
KeywordsSIGNALING PROTEIN/PEPTIDE INHIBITOR / RECEPTOR BINDING / REGULATORY / SIGNALING PROTEIN-SIGNALING PROTEIN INHIBITOR / SIGNALING PROTEIN-PEPTIDE INHIBITOR complex
Function / homology
Function and homology information


: / : / Regulation of T cell activation by CD28 family / : / Signaling by FGFR3 fusions in cancer / anatomical structure formation involved in morphogenesis / guanyl-nucleotide exchange factor adaptor activity / Grb2-EGFR complex / branching involved in labyrinthine layer morphogenesis / STAT5 Activation ...: / : / Regulation of T cell activation by CD28 family / : / Signaling by FGFR3 fusions in cancer / anatomical structure formation involved in morphogenesis / guanyl-nucleotide exchange factor adaptor activity / Grb2-EGFR complex / branching involved in labyrinthine layer morphogenesis / STAT5 Activation / Co-inhibition by BTLA / neurotrophin TRKA receptor binding / COP9 signalosome / Activated NTRK2 signals through PI3K / MET receptor recycling / transmembrane receptor protein tyrosine kinase adaptor activity / Signaling by cytosolic FGFR1 fusion mutants / Interleukin-15 signaling / negative regulation of natural killer cell mediated cytotoxicity / MET activates PTPN11 / MET activates RAP1 and RAC1 / vesicle membrane / Signaling by LTK / MET activates PI3K/AKT signaling / CD28 dependent Vav1 pathway / Signal regulatory protein family interactions / epidermal growth factor receptor binding / Regulation of KIT signaling / PI-3K cascade:FGFR3 / natural killer cell mediated cytotoxicity / STAT5 activation downstream of FLT3 ITD mutants / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / endodermal cell differentiation / positive regulation of actin filament polymerization / GRB2:SOS provides linkage to MAPK signaling for Integrins / RHOU GTPase cycle / regulation of MAPK cascade / RET signaling / insulin receptor substrate binding / Interleukin-3, Interleukin-5 and GM-CSF signaling / PI3K events in ERBB2 signaling / PI3K Cascade / signal transduction in response to DNA damage / SOS-mediated signalling / Role of LAT2/NTAL/LAB on calcium mobilization / fibroblast growth factor receptor signaling pathway / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / Interleukin receptor SHC signaling / SHC1 events in ERBB4 signaling / RHO GTPases Activate WASPs and WAVEs / Signal attenuation / Signalling to RAS / GAB1 signalosome / SHC-related events triggered by IGF1R / Activated NTRK2 signals through FRS2 and FRS3 / Schwann cell development / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / SHC-mediated cascade:FGFR2 / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / SHC-mediated cascade:FGFR4 / Erythropoietin activates RAS / SHC-mediated cascade:FGFR1 / Signaling by FGFR4 in disease / ephrin receptor binding / Signaling by CSF3 (G-CSF) / FRS-mediated FGFR3 signaling / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / FRS-mediated FGFR1 signaling / Tie2 Signaling / Signaling by FGFR2 in disease / phosphotyrosine residue binding / myelination / GRB2 events in EGFR signaling / Signaling by FLT3 fusion proteins / SHC1 events in EGFR signaling / FLT3 Signaling / Signaling by FGFR1 in disease / EGFR Transactivation by Gastrin / NCAM signaling for neurite out-growth / FCERI mediated Ca+2 mobilization / GRB2 events in ERBB2 signaling / Downstream signal transduction / insulin-like growth factor receptor signaling pathway / Insulin receptor signalling cascade / SHC1 events in ERBB2 signaling / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / Constitutive Signaling by Overexpressed ERBB2 / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / T cell activation / InlB-mediated entry of Listeria monocytogenes into host cell / cellular response to ionizing radiation / B cell receptor signaling pathway
Similarity search - Function
GRB2, N-terminal SH3 domain / GRB2, C-terminal SH3 domain / Grb2-like / SH2 domain / SHC Adaptor Protein / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain ...GRB2, N-terminal SH3 domain / GRB2, C-terminal SH3 domain / Grb2-like / SH2 domain / SHC Adaptor Protein / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / 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 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
MAZ-PY-(ALPHA ME)PY-N-NH2 / Growth factor receptor-bound protein 2 / Growth factor receptor-bound protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsNioche, P. / Liu, W.-Q. / Broutin, I. / Charbonnier, F. / Latreille, M.-T. / Vidal, M. / Roques, B. / Garbay, C. / Ducruix, A.
CitationJournal: J.Mol.Biol. / Year: 2002
Title: Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor.
Authors: Nioche, P. / Liu, W.Q. / Broutin, I. / Charbonnier, F. / Latreille, M.T. / Vidal, M. / Roques, B. / Garbay, C. / Ducruix, A.
History
DepositionSep 13, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 13, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary / Version format compliance
Revision 1.3Dec 12, 2012Group: Other
Revision 1.4Apr 4, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type
Revision 2.0Jul 10, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / struct_conn / struct_ref_seq_dif
Item: _chem_comp.formula / _chem_comp.formula_weight ..._chem_comp.formula / _chem_comp.formula_weight / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Revision 2.1Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
B: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
L: mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor
H: mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor


Theoretical massNumber of molelcules
Total (without water)23,7064
Polymers23,7064
Non-polymers00
Water2,990166
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4350 Å2
ΔGint-35 kcal/mol
Surface area9460 Å2
MethodPISA
2
A: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
B: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
L: mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor
H: mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor

A: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
B: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
L: mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor
H: mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor


Theoretical massNumber of molelcules
Total (without water)47,4138
Polymers47,4138
Non-polymers00
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation12_565x,x-y+1,-z+1/61
Buried area10100 Å2
ΔGint-79 kcal/mol
Surface area17520 Å2
MethodPISA
Unit cell
Length a, b, c (Å)60.999, 60.999, 177.046
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

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Components

#1: Protein GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 / GRB2 ADAPTER PROTEIN


Mass: 11071.563 Da / Num. of mol.: 2 / Fragment: SH2 Domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P29354, UniProt: P62993*PLUS
#2: Protein/peptide mAZ-pY-(alpha Me)pY-N-NH2 peptide inhibitor


Type: Peptide-like / Class: Inhibitor / Mass: 781.597 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: This peptide was chemically synthesized / References: MAZ-PY-(ALPHA ME)PY-N-NH2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 166 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.01 Å3/Da / Density % sol: 38.74 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6
Details: Ammonium phosphate, PEG400, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Crystal grow
*PLUS
Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
12.3 Mammonium phosphate11
24 %(w/v)PEG40011
350 mMsodium cacodylate11
419 mg/mlprotein11

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Type: ESRF / Wavelength: 0.933 Å
DetectorDetector: CCD / Date: Sep 23, 1999
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionHighest resolution: 2 Å / Num. all: 14016 / Num. obs: 13295 / % possible obs: 99.8 % / Biso Wilson estimate: 10.7 Å2 / Rsym value: 0.057
Reflection
*PLUS
Num. obs: 14016 / Num. measured all: 434272 / Rmerge(I) obs: 0.057
Reflection shell
*PLUS
% possible obs: 100 % / Rmerge(I) obs: 0.095

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Processing

Software
NameVersionClassification
AMoREphasing
CNS1refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→7.98 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 1807484.3 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 3 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.251 987 7.4 %RANDOM
Rwork0.185 ---
all-14016 --
obs-13295 96.9 %-
Displacement parametersBiso mean: 17.4 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.26 Å0.18 Å
Luzzati d res low-5 Å
Luzzati sigma a0.03 Å-0.07 Å
Refinement stepCycle: LAST / Resolution: 2→7.98 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1672 0 0 166 1838
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.027
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg2.2
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d25.3
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d2.09
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it1.551.5
X-RAY DIFFRACTIONc_mcangle_it2.262
X-RAY DIFFRACTIONc_scbond_it2.32
X-RAY DIFFRACTIONc_scangle_it3.22.5
LS refinement shellResolution: 2→2.12 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.205 161 7.6 %
Rwork0.138 1948 -
obs--94.9 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION3bond-maz-ptr.parambond-maz-ptr.top
Refinement
*PLUS
Highest resolution: 2 Å / Lowest resolution: 8 Å / σ(F): 3 / % reflection Rfree: 7.4 % / Rfactor obs: 0.185
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 17.4 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg25.3
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg2.09
X-RAY DIFFRACTIONc_mcbond_it1.551.5
X-RAY DIFFRACTIONc_scbond_it2.32
X-RAY DIFFRACTIONc_mcangle_it2.262
X-RAY DIFFRACTIONc_scangle_it3.22.5
LS refinement shell
*PLUS
Rfactor Rfree: 0.205 / % reflection Rfree: 7.6 % / Rfactor Rwork: 0.138

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