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- PDB-5xmt: Plasmodium vivax SHMT bound with PLP-glycine and GS380 -

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Basic information

Entry
Database: PDB / ID: 5xmt
TitlePlasmodium vivax SHMT bound with PLP-glycine and GS380
ComponentsSerine hydroxymethyltransferase
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / alpha and beta protein / methyltransferase activity / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information


glycine hydroxymethyltransferase / glycine hydroxymethyltransferase activity / glycine biosynthetic process from serine / tetrahydrofolate interconversion / methyltransferase activity / pyridoxal phosphate binding / methylation
Similarity search - Function
: / Serine hydroxymethyltransferase / Serine hydroxymethyltransferase-like domain / Serine hydroxymethyltransferase / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain ...: / Serine hydroxymethyltransferase / Serine hydroxymethyltransferase-like domain / Serine hydroxymethyltransferase / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-8B0 / Chem-PLG / glycine hydroxymethyltransferase / glycine hydroxymethyltransferase
Similarity search - Component
Biological speciesPlasmodium vivax (malaria parasite P. vivax)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
Model detailsPlasmodium vivax SHMT bound with PLP-glycine and GS362
AuthorsChitnumsub, P. / Jaruwat, A. / Leartsakulpanich, U. / Schwertz, G. / Diederich, F.
Funding support Thailand, 2items
OrganizationGrant numberCountry
National Science and Technology development AgencyCPMO-P-13-00835 Thailand
National Center for Genetic Engineering and BiotechnologyPlatform P-14-50241 Thailand
CitationJournal: Chemistry / Year: 2017
Title: Conformational Aspects in the Design of Inhibitors for Serine Hydroxymethyltransferase (SHMT): Biphenyl, Aryl Sulfonamide, and Aryl Sulfone Motifs
Authors: Schwertz, G. / Frei, M.S. / Witschel, M.C. / Rottmann, M. / Leartsakulpanich, U. / Chitnumsub, P. / Jaruwat, A. / Ittarat, W. / Schafer, A. / Aponte, R.A. / Trapp, N. / Mark, K. / Chaiyen, P. / Diederich, F.
History
DepositionMay 16, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 29, 2017Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
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: Serine hydroxymethyltransferase
B: Serine hydroxymethyltransferase
C: Serine hydroxymethyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)150,12711
Polymers147,7473
Non-polymers2,3808
Water5,531307
1
A: Serine hydroxymethyltransferase
B: Serine hydroxymethyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,0737
Polymers98,4982
Non-polymers1,5755
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10280 Å2
ΔGint-56 kcal/mol
Surface area29820 Å2
MethodPISA
2
C: Serine hydroxymethyltransferase
hetero molecules

C: Serine hydroxymethyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,1098
Polymers98,4982
Non-polymers1,6106
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area9500 Å2
ΔGint-57 kcal/mol
Surface area29690 Å2
MethodPISA
Unit cell
Length a, b, c (Å)101.578, 58.613, 236.371
Angle α, β, γ (deg.)90.000, 89.970, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11C-503-

CL

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Components

#1: Protein Serine hydroxymethyltransferase


Mass: 49249.160 Da / Num. of mol.: 3 / Fragment: RESIDUES 1-442
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium vivax (malaria parasite P. vivax)
Gene: PVC01_140059500, PVP01_1453700, PVT01_140059000 / Plasmid: pET17b / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)
References: UniProt: A0A1G4H5I1, UniProt: A5K8L9*PLUS, glycine hydroxymethyltransferase
#2: Chemical ChemComp-PLG / N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] / N-PYRIDOXYL-GLYCINE-5-MONOPHOSPHATE


Mass: 306.209 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H15N2O7P
#3: Chemical ChemComp-8B0 / (4~{S})-6-azanyl-4-[3-(2-cyanophenyl)-5-(trifluoromethyl)phenyl]-3-methyl-4-propan-2-yl-2~{H}-pyrano[2,3-c]pyrazole-5-carbonitrile / (s)-6-amino-4-(2'-cyano-5-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)-4-isopropyl-3-methyl-2,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile


Mass: 463.454 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C25H20F3N5O
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 307 / 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: 2.38 Å3/Da / Density % sol: 48.35 % / Mosaicity: 0.432 °
Crystal growTemperature: 298 K / Method: microbatch / pH: 8.5 / Details: PEG4000, 0.06-0.12M NaCl, 0.1M Tris-HCl pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 14, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.55→30 Å / Num. obs: 42088 / % possible obs: 92.3 % / Redundancy: 4.9 % / Rmerge(I) obs: 0.027 / Rpim(I) all: 0.012 / Rrim(I) all: 0.03 / Χ2: 0.872 / Net I/σ(I): 27.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.55-2.644.70.0590.9970.0270.0650.67780.7
2.64-2.754.50.0510.9970.0240.0570.73681.9
2.75-2.874.40.0430.9980.0210.0480.884.3
2.87-3.024.30.0390.9980.0190.0430.85788.3
3.02-3.214.20.0320.9980.0150.0350.86693.4
3.21-3.464.30.0280.9980.0140.0320.90397.3
3.46-3.814.80.0260.9990.0130.0290.98398.5
3.81-4.365.40.0250.9990.0110.0270.98299.4
4.36-5.485.80.0280.9990.0120.0311.1999.2
5.48-3060.0190.9990.0080.0210.61599.1

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
REFMAC5.8.0103refinement
PDB_EXTRACT3.22data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4tmr

4tmr


Resolution: 2.55→30 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.876 / SU B: 11.861 / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.395
RfactorNum. reflection% reflectionSelection details
Rfree0.2716 4194 10 %RANDOM
Rwork0.1946 ---
obs0.2023 37865 92.11 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å
Displacement parametersBiso max: 96.87 Å2 / Biso mean: 32.648 Å2 / Biso min: 10.22 Å2
Baniso -1Baniso -2Baniso -3
1-0.08 Å20 Å2-0.07 Å2
2---0.27 Å2-0 Å2
3---0.19 Å2
Refinement stepCycle: final / Resolution: 2.55→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10374 0 164 307 10845
Biso mean--33.22 27.83 -
Num. residues----1326
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01910736
X-RAY DIFFRACTIONr_bond_other_d0.0020.0210341
X-RAY DIFFRACTIONr_angle_refined_deg1.4881.97614524
X-RAY DIFFRACTIONr_angle_other_deg0.986323811
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.40951323
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.61825.247486
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.624151911
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.1451548
X-RAY DIFFRACTIONr_chiral_restr0.0760.21611
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0212198
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022424
LS refinement shellResolution: 2.554→2.62 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.392 268 -
Rwork0.243 2386 -
all-2654 -
obs--80.87 %

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