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- PDB-5scj: Structure of liver pyruvate kinase in complex with anthraquinone ... -

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Basic information

Entry
Database: PDB / ID: 5scj
TitleStructure of liver pyruvate kinase in complex with anthraquinone derivative 106
ComponentsPyruvate kinase
KeywordsTRANSFERASE/TRANSFERASE inhibitor / Pyruvate kinase / active site / inhibition / TRANSFERASE / TRANSFERASE-TRANSFERASE inhibitor complex
Function / homology
Function and homology information


pyruvate kinase / pyruvate kinase activity / potassium ion binding / kinase activity / phosphorylation / magnesium ion binding / ATP binding
Similarity search - Function
Pyruvate kinase, active site / Pyruvate kinase active site signature. / Pyruvate kinase / Pyruvate kinase, barrel / Pyruvate kinase, insert domain superfamily / Pyruvate kinase, barrel domain / Pyruvate kinase, C-terminal / Pyruvate kinase, C-terminal domain superfamily / Pyruvate kinase, alpha/beta domain / Pyruvate kinase-like, insert domain superfamily ...Pyruvate kinase, active site / Pyruvate kinase active site signature. / Pyruvate kinase / Pyruvate kinase, barrel / Pyruvate kinase, insert domain superfamily / Pyruvate kinase, barrel domain / Pyruvate kinase, C-terminal / Pyruvate kinase, C-terminal domain superfamily / Pyruvate kinase, alpha/beta domain / Pyruvate kinase-like, insert domain superfamily / Pyruvate kinase-like domain superfamily / Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
Similarity search - Domain/homology
1,6-di-O-phosphono-beta-D-fructofuranose / Chem-I9K / : / OXALATE ION / Pyruvate kinase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / molecular replacement / Resolution: 2.354 Å
AuthorsLulla, A. / Foller, A. / Nain-Perez, A. / Grotli, M. / Brear, P. / Hyvonen, M.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Not funded United Kingdom
CitationJournal: Eur.J.Med.Chem. / Year: 2022
Title: Anthraquinone derivatives as ADP-competitive inhibitors of liver pyruvate kinase.
Authors: Nain-Perez, A. / Foller Fuchtbauer, A. / Haversen, L. / Lulla, A. / Gao, C. / Matic, J. / Monjas, L. / Rodriguez, A. / Brear, P. / Kim, W. / Hyvonen, M. / Boren, J. / Mardinoglu, A. / Uhlen, M. / Grotli, M.
History
DepositionDec 1, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 16, 2022Provider: repository / Type: Initial release
Revision 2.0Mar 30, 2022Group: Database references / Non-polymer description / Category: chem_comp / citation / citation_author
Item: _chem_comp.formula / _citation.country ..._chem_comp.formula / _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pyruvate kinase
B: Pyruvate kinase
C: Pyruvate kinase
D: Pyruvate kinase
E: Pyruvate kinase
F: Pyruvate kinase
G: Pyruvate kinase
H: Pyruvate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)392,40144
Polymers386,2838
Non-polymers6,11836
Water12,268681
1
A: Pyruvate kinase
B: Pyruvate kinase
C: Pyruvate kinase
D: Pyruvate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,20122
Polymers193,1424
Non-polymers3,05918
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21750 Å2
ΔGint-132 kcal/mol
Surface area56680 Å2
MethodPISA
2
E: Pyruvate kinase
F: Pyruvate kinase
G: Pyruvate kinase
H: Pyruvate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,20122
Polymers193,1424
Non-polymers3,05918
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21610 Å2
ΔGint-133 kcal/mol
Surface area55720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)208.143, 113.061, 188.959
Angle α, β, γ (deg.)90.000, 91.540, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Protein / Sugars , 2 types, 16 molecules ABCDEFGH

#1: Protein
Pyruvate kinase /


Mass: 48285.379 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pEXP-NHis / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q16716, pyruvate kinase
#2: Sugar
ChemComp-FBP / 1,6-di-O-phosphono-beta-D-fructofuranose / BETA-FRUCTOSE-1,6-DIPHOSPHATE / FRUCTOSE-1,6-BISPHOSPHATE / 1,6-di-O-phosphono-beta-D-fructose / 1,6-di-O-phosphono-D-fructose / 1,6-di-O-phosphono-fructose / Fructose 1,6-bisphosphate


Type: D-saccharide, beta linking / Mass: 340.116 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C6H14O12P2
IdentifierTypeProgram
b-D-Fruf1PO36PO3IUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 5 types, 709 molecules

#3: Chemical
ChemComp-OXL / OXALATE ION / Oxalate


Mass: 88.019 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2O4
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: K
#6: Chemical
ChemComp-I9K / (2R)-2-hydroxy-2-{2-[4-(3-hydroxy-9,10-dioxo-9,10-dihydroanthracene-2-sulfonyl)piperazin-1-yl]-2-oxoethyl}butanedioic acid


Mass: 546.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C24H22N2O11S / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 681 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.88 Å3/Da / Density % sol: 57.25 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 100 mM HEPES/MOPS, 10% PEG8000, 20% ethylene glycol, 10 mM phenylalanine, 20 mM sodium oxalate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 11, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 2.354→188.891 Å / Num. obs: 102770 / % possible obs: 88.4 % / Redundancy: 7 % / CC1/2: 0.998 / Rmerge(I) obs: 0.147 / Rpim(I) all: 0.06 / Net I/σ(I): 8.9 / Num. measured all: 714710
Reflection shell

Num. unique obs: 5138

Resolution (Å)% possible obs (%)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsCC1/2Rpim(I) all
2.354-2.63446.66.81.3731.7351020.5980.568
7.809-188.89199.87.20.0426.6369130.9990.016

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
XDSdata reduction
PHASERphasing
BUSTER2.10.4 (16-JUL-2021)refinement
PDB_EXTRACT3.25data extraction
STARANISOdata scaling
RefinementMethod to determine structure: molecular replacement / Resolution: 2.354→188.89 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.902 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.359
Details: HYDROGENS WERE FULLY REFINED WITH ZERO OCCUPANCY AT NUCLEAR POSITION. REFINEMENT NOTES. NUMBER OF REFINEMENT NOTES : 1 NOTE 1 : IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
RfactorNum. reflection% reflectionSelection details
Rfree0.253 4891 4.76 %RANDOM
Rwork0.2183 ---
obs0.2199 102769 56.7 %-
Displacement parametersBiso max: 140.54 Å2 / Biso mean: 58.59 Å2 / Biso min: 17.42 Å2
Baniso -1Baniso -2Baniso -3
1--0.9142 Å20 Å2-1.0733 Å2
2---0.5031 Å20 Å2
3---1.4173 Å2
Refine analyzeLuzzati coordinate error obs: 0.36 Å
Refinement stepCycle: final / Resolution: 2.354→188.89 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25843 0 376 681 26900
Biso mean--72.09 44.63 -
Num. residues----3405
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d9618SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes4800HARMONIC5
X-RAY DIFFRACTIONt_it26912HARMONIC10
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion3609SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact22980SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d26999HARMONIC20.008
X-RAY DIFFRACTIONt_angle_deg36707HARMONIC20.93
X-RAY DIFFRACTIONt_omega_torsion2.8
X-RAY DIFFRACTIONt_other_torsion16.88
LS refinement shellResolution: 2.35→2.54 Å / Rfactor Rfree error: 0 / Total num. of bins used: 51
RfactorNum. reflection% reflection
Rfree0.3122 84 4.09 %
Rwork0.2786 1972 -
all0.28 2056 -
obs--5.6 %

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