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- PDB-3oza: Crystal Structure of Plasmodium falciparum 3-Phosphoglycerate Kinase -

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Basic information

Entry
Database: PDB / ID: 3oza
TitleCrystal Structure of Plasmodium falciparum 3-Phosphoglycerate Kinase
ComponentsPhosphoglycerate kinase
KeywordsTRANSFERASE / Phosphoglycerate Kinase / Kinase / Nucleotide binding / ATP binding / Glycolysis / Malaraia Parasite
Function / homology
Function and homology information


Gluconeogenesis / Glycolysis / phosphoglycerate kinase / phosphoglycerate kinase activity / gluconeogenesis / glycolytic process / ADP binding / calmodulin binding / phosphorylation / ATP binding / cytosol
Similarity search - Function
Phosphoglycerate kinase, N-terminal domain / Phosphoglycerate kinase / Phosphoglycerate kinase, N-terminal / Phosphoglycerate kinase, conserved site / Phosphoglycerate kinase superfamily / Phosphoglycerate kinase / Phosphoglycerate kinase signature. / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Phosphoglycerate kinase
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3 Å
AuthorsSmith, C.D. / Chattopadhyay, D. / Pal, B.
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2011
Title: Crystal structure of Plasmodium falciparum phosphoglycerate kinase: Evidence for anion binding in the basic patch.
Authors: Smith, C.D. / Chattopadhyay, D. / Pal, B.
History
DepositionSep 24, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 24, 2011Provider: repository / Type: Initial release
Revision 1.1Sep 14, 2011Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Phosphoglycerate kinase
B: Phosphoglycerate kinase
C: Phosphoglycerate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)141,4659
Polymers140,8973
Non-polymers5686
Water82946
1
A: Phosphoglycerate kinase
B: Phosphoglycerate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,4037
Polymers93,9312
Non-polymers4725
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5270 Å2
ΔGint-54 kcal/mol
Surface area33510 Å2
MethodPISA
2
C: Phosphoglycerate kinase
hetero molecules

C: Phosphoglycerate kinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,1234
Polymers93,9312
Non-polymers1922
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_565-x,-y+1,z1
Buried area4670 Å2
ΔGint-39 kcal/mol
Surface area33780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.030, 147.610, 206.490
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

#1: Protein Phosphoglycerate kinase


Mass: 46965.551 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Strain: 3D7 / Gene: PGK, PFI1105w / Production host: Escherichia coli (E. coli) / References: UniProt: P27362, phosphoglycerate kinase
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 46 / Source method: isolated from a natural source / Formula: H2O

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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: 3.22 Å3/Da / Density % sol: 61.79 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: AMMONIUM SULFATE, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 0.9793, 0.9792, 0.9537
DetectorType: MARRESEARCH / Detector: CCD / Date: Jun 17, 2001
RadiationMonochromator: DOUBLE CRYSTAL SILICON / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.97931
20.97921
30.95371
ReflectionResolution: 3→19.93 Å / Num. all: 36622 / Num. obs: 34736 / % possible obs: 94.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0

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Processing

Software
NameVersionClassificationNB
REFMACrefinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
HKL-2000data reduction
SCALEPACKdata scaling
SOLVEphasing
RefinementMethod to determine structure: MAD / Resolution: 3→19.93 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.871 / Occupancy max: 1 / Occupancy min: 1 / SU B: 18.251 / SU ML: 0.333 / Cross valid method: THROUGHOUT / ESU R Free: 0.478 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27138 3457 10 %RANDOM
Rwork0.20031 ---
obs0.2072 31275 94.84 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 54.719 Å2
Baniso -1Baniso -2Baniso -3
1--0.25 Å20 Å20 Å2
2--0.94 Å20 Å2
3----0.69 Å2
Refinement stepCycle: LAST / Resolution: 3→19.93 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9636 0 32 46 9714
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0229794
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1661.97913178
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.52151253
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.83926.536407
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.657151896
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.7541524
X-RAY DIFFRACTIONr_chiral_restr0.080.21523
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0217094
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4171.56203
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.8129980
X-RAY DIFFRACTIONr_scbond_it1.12133591
X-RAY DIFFRACTIONr_scangle_it1.9354.53198
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3→3.076 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.311 190 -
Rwork0.247 1954 -
obs--82.3 %

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