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- PDB-7jif: HRAS A59T GppNHp -

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Basic information

Entry
Database: PDB / ID: 7jif
TitleHRAS A59T GppNHp
ComponentsGTPase HRas
KeywordsONCOPROTEIN / Mutant Cancer GTPase
Function / homology
Function and homology information


phospholipase C activator activity / GTPase complex / positive regulation of ruffle assembly / oncogene-induced cell senescence / negative regulation of GTPase activity / positive regulation of miRNA metabolic process / T-helper 1 type immune response / positive regulation of wound healing / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / defense response to protozoan ...phospholipase C activator activity / GTPase complex / positive regulation of ruffle assembly / oncogene-induced cell senescence / negative regulation of GTPase activity / positive regulation of miRNA metabolic process / T-helper 1 type immune response / positive regulation of wound healing / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / defense response to protozoan / Signaling by RAS GAP mutants / Signaling by RAS GTPase mutants / Activation of RAS in B cells / RAS signaling downstream of NF1 loss-of-function variants / SOS-mediated signalling / Activated NTRK3 signals through RAS / positive regulation of protein targeting to membrane / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / Signalling to RAS / adipose tissue development / Activated NTRK2 signals through FRS2 and FRS3 / SHC-related events triggered by IGF1R / Estrogen-stimulated signaling through PRKCZ / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / Schwann cell development / SHC-mediated cascade:FGFR2 / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / SHC-mediated cascade:FGFR4 / Signaling by FGFR4 in disease / Erythropoietin activates RAS / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR3 signaling / Signaling by FLT3 ITD and TKD mutants / membrane-membrane adaptor activity / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / p38MAPK events / Tie2 Signaling / FRS-mediated FGFR1 signaling / Signaling by FGFR2 in disease / GRB2 events in EGFR signaling / EPHB-mediated forward signaling / SHC1 events in EGFR signaling / Signaling by FLT3 fusion proteins / FLT3 Signaling / Signaling by FGFR1 in disease / myelination / EGFR Transactivation by Gastrin / NCAM signaling for neurite out-growth / positive regulation of MAP kinase activity / CD209 (DC-SIGN) signaling / GRB2 events in ERBB2 signaling / Ras activation upon Ca2+ influx through NMDA receptor / Downstream signal transduction / SHC1 events in ERBB2 signaling / Insulin receptor signalling cascade / intrinsic apoptotic signaling pathway / positive regulation of GTPase activity / Constitutive Signaling by Overexpressed ERBB2 / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / VEGFR2 mediated cell proliferation / positive regulation of epithelial cell proliferation / small monomeric GTPase / animal organ morphogenesis / regulation of actin cytoskeleton organization / FCERI mediated MAPK activation / positive regulation of JNK cascade / RAF activation / regulation of long-term neuronal synaptic plasticity / Signaling by ERBB2 TMD/JMD mutants / Signaling by high-kinase activity BRAF mutants / Signaling by SCF-KIT / MAP2K and MAPK activation / Constitutive Signaling by EGFRvIII / cellular response to gamma radiation / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / positive regulation of type II interferon production / endocytosis / positive regulation of fibroblast proliferation / Regulation of RAS by GAPs / RAS processing / Signaling by RAF1 mutants / chemotaxis / Negative regulation of MAPK pathway / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / GDP binding / MAPK cascade / cellular senescence / Signaling by BRAF and RAF1 fusions / insulin receptor signaling pathway / DAP12 signaling / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
Similarity search - Function
Small GTPase, Ras-type / small GTPase Ras family profile. / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold ...Small GTPase, Ras-type / small GTPase Ras family profile. / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GTPase HRas
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.757 Å
AuthorsJohnson, C.W. / Haigis, K.M.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)R01CA230718 United States
American Cancer Society30428-PF-17-066-01-TBG United States
CitationJournal: Mol.Cell / Year: 2022
Title: Regulation of GTPase function by autophosphorylation.
Authors: Johnson, C.W. / Seo, H.S. / Terrell, E.M. / Yang, M.H. / KleinJan, F. / Gebregiworgis, T. / Gasmi-Seabrook, G.M.C. / Geffken, E.A. / Lakhani, J. / Song, K. / Bashyal, P. / Popow, O. / Paulo, ...Authors: Johnson, C.W. / Seo, H.S. / Terrell, E.M. / Yang, M.H. / KleinJan, F. / Gebregiworgis, T. / Gasmi-Seabrook, G.M.C. / Geffken, E.A. / Lakhani, J. / Song, K. / Bashyal, P. / Popow, O. / Paulo, J.A. / Liu, A. / Mattos, C. / Marshall, C.B. / Ikura, M. / Morrison, D.K. / Dhe-Paganon, S. / Haigis, K.M.
History
DepositionJul 23, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 2, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 9, 2022Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Mar 16, 2022Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.page_first
Revision 1.3Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GTPase HRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,5444
Polymers18,9051
Non-polymers6393
Water2,792155
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)39.567, 39.567, 158.302
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein GTPase HRas / H-Ras-1 / Ha-Ras / Transforming protein p21 / c-H-ras / p21ras


Mass: 18905.219 Da / Num. of mol.: 1 / Mutation: A59T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HRAS, HRAS1 / Production host: Escherichia coli #1/H766 (bacteria) / References: UniProt: P01112
#2: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3 / Feature type: SUBJECT OF INVESTIGATION
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 155 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 1.89 Å3/Da / Density % sol: 34.99 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: Starting concentration of HRAS A59T GppNHp was 12.1mg/mL in buffer containing 20mM HEPES, 50mM NaCl, 20mM MgCl2 and 1mM DTT at pH 7.5. Used a 24-well plate sealed with Vaseline and total ...Details: Starting concentration of HRAS A59T GppNHp was 12.1mg/mL in buffer containing 20mM HEPES, 50mM NaCl, 20mM MgCl2 and 1mM DTT at pH 7.5. Used a 24-well plate sealed with Vaseline and total well volumes of 0.402mL. Hanging drops were 0.002mL mother liquor to 0.002mL protein. Mother liquor contained 2.6mM NaCl, 1mM MgCl2, 15.7mM HEPES (pH7.5), 2.5mM DTT, 37.3mM Ca(OAc)2, and 20.5% PEG 3350

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Data collection

DiffractionMean temperature: 173.15 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54178 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: May 14, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54178 Å / Relative weight: 1
ReflectionResolution: 1.75→50 Å / Num. obs: 10520 / % possible obs: 68.1 % / Redundancy: 4.3 % / Biso Wilson estimate: 24.59 Å2 / Rmerge(I) obs: 0.032 / Rpim(I) all: 0.016 / Rrim(I) all: 0.036 / Χ2: 1.335 / Net I/σ(I): 29 / Num. measured all: 45757
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.75-1.781.20.378910.3780.5350.2521.2
1.78-1.811.40.235800.8710.1940.3060.91710.3
1.81-1.851.70.2141550.8350.1710.2760.79821.8
1.85-1.891.90.1992440.8780.1520.2531.02831
1.89-1.931.90.1792150.8890.1410.2311.46230.3
1.93-1.972.40.1783610.9430.1250.221.51346
1.97-2.022.70.1414250.9690.0940.1721.18556.4
2.02-2.072.60.1314620.9660.090.1611.66560.5
2.07-2.143.50.1085680.9770.0670.1291.6177
2.14-2.24.50.0897040.9870.050.1031.60891.7
2.2-2.283.20.0695600.9920.0420.0821.61474.6
2.28-2.384.20.0566970.9950.0320.0651.40293.3
2.38-2.484.20.0477360.9970.0270.0541.34993.3
2.48-2.614.40.0437260.9970.0240.0491.28894.5
2.61-2.784.20.0377120.9970.0210.0431.28794.1
2.78-2.994.90.037610.9980.0160.0341.13396.3
2.99-3.295.40.0277700.9990.0130.031.14498.1
3.29-3.775.20.0287450.9980.0140.0321.27594.3
3.77-4.755.80.0277400.9990.0120.031.3191.1
4.75-507.10.0288500.9990.0120.031.34893.9

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
HKL-3000data scaling
PDB_EXTRACT3.25data extraction
HKL-3000data reduction
PHENIX1.11.1-2575phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1CTQ

1ctq


Resolution: 1.757→33.49 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 29.03 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2498 1047 9.99 %random selection
Rwork0.1716 9434 --
obs0.1796 10481 69.08 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 55.57 Å2 / Biso mean: 23.1735 Å2 / Biso min: 12.39 Å2
Refinement stepCycle: final / Resolution: 1.757→33.49 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1315 0 39 155 1509
Biso mean--20.41 28.39 -
Num. residues----166
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0061402
X-RAY DIFFRACTIONf_angle_d0.9151909
X-RAY DIFFRACTIONf_chiral_restr0.05215
X-RAY DIFFRACTIONf_plane_restr0.004244
X-RAY DIFFRACTIONf_dihedral_angle_d11.6641156
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.7572-1.84980.5502240.354424013
1.8498-1.96570.446760.26569136
1.9657-2.11740.32281180.2338117062
2.1174-2.33050.29761880.1966166686
2.3305-2.66760.26362010.1848180794
2.6676-3.36030.24282100.1566189897
3.3603-33.490.21352300.1515196293

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