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- PDB-6eck: Pyruvate Kinase Isoform L-type with phosphorylated Ser113 (pS113)... -

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Basic information

Entry
Database: PDB / ID: 6eck
TitlePyruvate Kinase Isoform L-type with phosphorylated Ser113 (pS113) in complex with FBP
ComponentsPyruvate kinase PKLR
KeywordsTRANSFERASE / PKL / pyruvate kinase / Glycolysis
Function / homology
Function and homology information


Glycolysis / pyruvate biosynthetic process / ATP biosynthetic process / pyruvate kinase / pyruvate kinase activity / response to other organism / response to metal ion / monosaccharide binding / response to ATP / response to lithium ion ...Glycolysis / pyruvate biosynthetic process / ATP biosynthetic process / pyruvate kinase / pyruvate kinase activity / response to other organism / response to metal ion / monosaccharide binding / response to ATP / response to lithium ion / potassium ion binding / response to glucose / response to cAMP / cellular response to epinephrine stimulus / response to nutrient / glycolytic process / cellular response to insulin stimulus / kinase activity / response to heat / carbohydrate metabolic process / response to hypoxia / magnesium ion binding / ATP binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Pyruvate kinase, C-terminal domain / Pyruvate Kinase; Chain: A, domain 1 / 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, C-terminal domain / Pyruvate Kinase; Chain: A, domain 1 / 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 / Phosphoenolpyruvate-binding domains / Pyruvate kinase-like domain superfamily / Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily / TIM Barrel / Alpha-Beta Barrel / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
1,6-di-O-phosphono-beta-D-fructofuranose / CITRATE ANION / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / Pyruvate kinase PKLR
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.36 Å
AuthorsPadyana, A. / Tong, S.
CitationJournal: Cell Rep / Year: 2019
Title: Distinct Hepatic PKA and CDK Signaling Pathways Control Activity-Independent Pyruvate Kinase Phosphorylation and Hepatic Glucose Production.
Authors: Gassaway, B.M. / Cardone, R.L. / Padyana, A.K. / Petersen, M.C. / Judd, E.T. / Hayes, S. / Tong, S. / Barber, K.W. / Apostolidi, M. / Abulizi, A. / Sheetz, J.B. / Aerni, H.R. / Gross, S. / ...Authors: Gassaway, B.M. / Cardone, R.L. / Padyana, A.K. / Petersen, M.C. / Judd, E.T. / Hayes, S. / Tong, S. / Barber, K.W. / Apostolidi, M. / Abulizi, A. / Sheetz, J.B. / Aerni, H.R. / Gross, S. / Kung, C. / Samuel, V.T. / Shulman, G.I. / Kibbey, R.G. / Rinehart, J.
History
DepositionAug 8, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 4, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 25, 2019Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pyruvate kinase PKLR
B: Pyruvate kinase PKLR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,51514
Polymers119,8212
Non-polymers1,69412
Water6,972387
1
A: Pyruvate kinase PKLR
B: Pyruvate kinase PKLR
hetero molecules

A: Pyruvate kinase PKLR
B: Pyruvate kinase PKLR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)243,03028
Polymers239,6424
Non-polymers3,38824
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-x+1,-y+1,z1
Buried area26370 Å2
ΔGint-63 kcal/mol
Surface area76130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.774, 111.843, 127.507
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-767-

HOH

21A-907-

HOH

31B-780-

HOH

41B-804-

HOH

51B-857-

HOH

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Components

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Protein / Sugars , 2 types, 4 molecules AB

#1: Protein Pyruvate kinase PKLR / L-PK / Pyruvate kinase isozymes L/R


Mass: 59910.461 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Pklr / Production host: Escherichia coli (E. coli) / Strain (production host): Recoded / Variant (production host): C321-deltaA / References: UniProt: P12928, 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


Type: D-saccharide, beta linking / Mass: 340.116 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C6H14O12P2
IdentifierTypeProgram
b-D-Fruf1PO36PO3IUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 6 types, 397 molecules

#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3
#5: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-FLC / CITRATE ANION


Mass: 189.100 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H5O7
#7: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 387 / 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: 2.92 Å3/Da / Density % sol: 57.82 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.1 M HEPES, pH 7.5, 10% ethylene glycol, 12% PEG8000
PH range: 7.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9778 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 6, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9778 Å / Relative weight: 1
ReflectionResolution: 2.36→48.59 Å / Num. obs: 56712 / % possible obs: 97.9 % / Redundancy: 6.2 % / CC1/2: 0.994 / Rmerge(I) obs: 0.147 / Rpim(I) all: 0.066 / Rrim(I) all: 0.162 / Net I/σ(I): 7.8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.36-2.436.61.242930.750.51.30292
10.02-48.545.80.068470.9950.0270.06798.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
HKL-20002000data reduction
Aimless0.7.2data scaling
PHASER2.7.0phasing
REFMAC5.8.0230refinement
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 4IP7

4ip7


Resolution: 2.36→48.59 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.908 / SU B: 9.992 / SU ML: 0.225 / SU R Cruickshank DPI: 0.3293 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.329 / ESU R Free: 0.267
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.275 2815 5 %RANDOM
Rwork0.2035 ---
obs0.207 53862 97.56 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 220.61 Å2 / Biso mean: 59.669 Å2 / Biso min: 23.65 Å2
Baniso -1Baniso -2Baniso -3
1--4.53 Å2-0 Å20 Å2
2--2.58 Å2-0 Å2
3---1.95 Å2
Refinement stepCycle: final / Resolution: 2.36→48.59 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8083 0 117 387 8587
Biso mean--63.28 52.97 -
Num. residues----1060
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0148369
X-RAY DIFFRACTIONr_bond_other_d0.0010.0177756
X-RAY DIFFRACTIONr_angle_refined_deg1.561.66511329
X-RAY DIFFRACTIONr_angle_other_deg0.9021.64518160
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.16751065
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.56521.054427
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.257151436
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.9541575
X-RAY DIFFRACTIONr_chiral_restr0.0710.21128
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.029395
X-RAY DIFFRACTIONr_gen_planes_other0.0020.021417
LS refinement shellResolution: 2.361→2.423 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.397 180 -
Rwork0.342 3670 -
all-3850 -
obs--91.12 %

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