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- PDB-5qt9: T. brucei FPPS in complex with CID 23155989 -

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Basic information

Entry
Database: PDB / ID: 5qt9
TitleT. brucei FPPS in complex with CID 23155989
ComponentsFarnesyl pyrophosphate synthaseDimethylallyltranstransferase
KeywordsTRANSFERASE/TRANSFERASE inhibitor / farnesyl diphosphate synthase / Trypanosoma brucei / PanDDA / protein-ligand complex / TRANSFERASE-TRANSFERASE inhibitor complex
Function / homology
Function and homology information


transferase activity, transferring alkyl or aryl (other than methyl) groups / isoprenoid biosynthetic process / metal ion binding
Similarity search - Function
Farnesyl pyrophosphate synthase-like / Polyprenyl synthases signature 1. / Polyprenyl synthases signature 2. / Polyprenyl synthetase, conserved site / Polyprenyl synthetase / Polyprenyl synthetase / Isoprenoid synthase domain superfamily
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Chem-PJ4 / Farnesyl pyrophosphate synthase
Similarity search - Component
Biological speciesTrypanosoma brucei (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.199 Å
AuthorsMuenzker, L. / Petrick, J.K. / Schleberger, C. / Jahnke, W.
CitationJournal: To Be Published
Title: T. brucei FPPS in complex with CID 23155989
Authors: Muenzker, L.
History
DepositionAug 7, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Farnesyl pyrophosphate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,6174
Polymers42,1691
Non-polymers4483
Water59433
1
A: Farnesyl pyrophosphate synthase
hetero molecules

A: Farnesyl pyrophosphate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,2348
Polymers84,3382
Non-polymers8966
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_555x-y,-y,-z1
Buried area6260 Å2
ΔGint-19 kcal/mol
Surface area27460 Å2
MethodPISA
Unit cell
Length a, b, c (Å)60.929, 60.929, 343.320
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11A-511-

HOH

21A-517-

HOH

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Components

#1: Protein Farnesyl pyrophosphate synthase / Dimethylallyltranstransferase


Mass: 42169.211 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trypanosoma brucei (eukaryote) / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q86C09
#2: Chemical ChemComp-PJ4 / (1S)-3-chloro-1-(4-methylpiperazin-1-yl)-1,4-dihydroisoquinoline


Mass: 263.766 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H18ClN3 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#4: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 33 / 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: 2.18 Å3/Da / Density % sol: 43.61 % / Mosaicity: 0.08 °
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 / Details: 0.12 M CsCl 12 % w/v PEG 3350, 6 % v/v xylitol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99997 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Mar 26, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99997 Å / Relative weight: 1
ReflectionResolution: 2.199→52.766 Å / Num. obs: 12144 / % possible obs: 59.4 % / Redundancy: 17.9 % / CC1/2: 0.999 / Rmerge(I) obs: 0.125 / Rpim(I) all: 0.04 / Rrim(I) all: 0.172 / Rsym value: 0.125 / Net I/σ(I): 16.3 / Num. measured all: 299421 / Scaling rejects: 1
Reflection shellResolution: 2.199→2.475 Å / Redundancy: 16 % / Rmerge(I) obs: 1.543 / Mean I/σ(I) obs: 1.9 / Num. measured all: 46150 / Num. unique obs: 2347 / CC1/2: 0.553 / Rpim(I) all: 1.598 / Rrim(I) all: 7.189 / Rsym value: 1.543 / Net I/σ(I) obs: 0.6 / % possible all: 10.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIX1.14_3260refinement
Aimless0.7.4data scaling
XDS20180808data reduction
PHASER2.8.2phasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdbid 4ryp

4ryp


Resolution: 2.199→52.766 Å / SU ML: 0.23 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 34.1 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2742 620 5.11 %
Rwork0.2295 11517 -
obs0.2318 12137 59.32 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 176.45 Å2 / Biso mean: 66.0908 Å2 / Biso min: 16.13 Å2
Refinement stepCycle: final / Resolution: 2.199→52.766 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2595 0 29 33 2657
Biso mean--78.3 52.05 -
Num. residues----325
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.1989-2.42010.3689220.3513854078
2.4201-2.77030.3472950.32791530162532
2.7703-3.49020.32172380.27824561479995
3.4902-52.78120.24652650.20125041530697

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