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- PDB-7ok4: Crystal Structure of KRasG13C in Complex with Nucleotide-based co... -

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Basic information

Entry
Database: PDB / ID: 7ok4
TitleCrystal Structure of KRasG13C in Complex with Nucleotide-based covalent Inhibitor bdaGDP
ComponentsIsoform 2B of GTPase KRas
KeywordsHYDROLASE / GTPase / Ras / KRas / KRasG13C / Nucleotide analogues / bdaGDP
Function / homologysmall monomeric GTPase / Ca2+ pathway / bdaGDP / Isoform 2B of GTPase KRas
Function and homology information
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsGoebel, L. / Mueller, M.P. / Rauh, D.
Funding support Germany, 2items
OrganizationGrant numberCountry
German Research Foundation (DFG)RA 1055/5-1 Germany
German Research Foundation (DFG)GO 284/10-1 Germany
CitationJournal: Elife / Year: 2023
Title: Targeting oncogenic KRasG13C with nucleotide-based covalent inhibitors.
Authors: Goebel, L. / Kirschner, T. / Koska, S. / Rai, A. / Janning, P. / Maffini, S. / Vatheuer, H. / Czodrowski, P. / Goody, R.S. / Muller, M.P. / Rauh, D.
History
DepositionMay 17, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 3, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 29, 2023Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.year
Revision 1.2Apr 5, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Feb 7, 2024Group: 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: Isoform 2B of GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,0472
Polymers19,4341
Non-polymers6131
Water1,910106
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area8380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)73.900, 73.900, 54.800
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number173
Space group name H-MP63
Components on special symmetry positions
IDModelComponents
11A-406-

HOH

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Components

#1: Protein Isoform 2B of GTPase KRas / K-Ras 2 / Ki-Ras / c-K-ras / c-Ki-ras


Mass: 19433.881 Da / Num. of mol.: 1 / Mutation: G13C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KRAS, KRAS2, RASK2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P01116-2, small monomeric GTPase
#2: Chemical ChemComp-VJB / bdaGDP / [(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanylidene-3~{H}-purin-9-yl)-4-oxidanyl-2-[[oxidanyl(phosphonooxy)phosphoryl]oxymethyl]oxolan-3-yl] ~{N}-[4-(propanoylamino)butyl]carbamate


Mass: 613.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H29N7O13P2 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 106 / 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: 2.22 Å3/Da / Density % sol: 44.66 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.2 M (NH4)F, 20 % PEG3350, 70 mg/mL KRas-bdaGDP, 0.1 uL reservoir + 0.1 uL protein solution

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9999 Å
DetectorType: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Mar 31, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9999 Å / Relative weight: 1
ReflectionResolution: 1.7→41.63 Å / Num. obs: 18838 / % possible obs: 100 % / Redundancy: 20.3 % / CC1/2: 1 / Rmerge(I) obs: 0.07 / Rrim(I) all: 0.071 / Net I/σ(I): 24.52
Reflection shellResolution: 1.7→1.8 Å / Rmerge(I) obs: 1.557 / Num. unique obs: 2948 / CC1/2: 0.784 / Rrim(I) all: 1.596 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.19.1_4122refinement
PDB_EXTRACTdata extraction
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4OBE

4obe


Resolution: 1.7→41.63 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 21.16 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1824 942 5 %
Rwork0.1653 17896 -
obs0.1661 18838 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 109.2 Å2 / Biso mean: 37.3486 Å2 / Biso min: 19.07 Å2
Refinement stepCycle: final / Resolution: 1.7→41.63 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1324 0 40 106 1470
Biso mean--30.77 44.99 -
Num. residues----170
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 7 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
1.7-1.790.35581330.264325322665
1.79-1.90.23841340.217325462680
1.9-2.050.2191340.183825482682
2.05-2.250.19311340.170125392673
2.25-2.580.22181340.173525472681
2.58-3.250.18761350.170525702705
3.25-41.630.14431380.145426142752
Refinement TLS params.Method: refined / Origin x: 27.4093 Å / Origin y: -5.3279 Å / Origin z: 9.8218 Å
111213212223313233
T0.2081 Å20.008 Å20.0185 Å2-0.2077 Å20.0094 Å2--0.2176 Å2
L1.7321 °20.2167 °20.6928 °2-2.8679 °20.7599 °2--2.3897 °2
S-0.0627 Å °-0.1029 Å °0.0743 Å °0.0088 Å °0.086 Å °0.2464 Å °-0.0858 Å °-0.143 Å °-0.0251 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allA0 - 169
2X-RAY DIFFRACTION1allB201
3X-RAY DIFFRACTION1allS1 - 106

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