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- PDB-3h2a: Structural Studies of Pterin-Based Inhibitors of Dihydropteroate ... -

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Basic information

Entry
Database: PDB / ID: 3h2a
TitleStructural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase
ComponentsDihydropteroate synthase
KeywordsTransferase/Transferase Inhibitor / ANTHRACIS / FOLATE BIOSYNTHESIS / DIHYDROPTEROATE / PTERINE / Transferase / Transferase-Transferase Inhibitor COMPLEX
Function / homology
Function and homology information


dihydropteroate synthase / dihydropteroate synthase activity / folic acid biosynthetic process / tetrahydrofolate biosynthetic process / metal ion binding
Similarity search - Function
Dihydropteroate synthase signature 1. / Dihydropteroate synthase / Dihydropteroate synthase domain / Dihydropteroate synthase signature 2. / Dihydropteroate synthase-like / Pterin-binding domain / Pterin binding enzyme / Pterin-binding domain profile. / Dihydropteroate synthase-like / TIM Barrel ...Dihydropteroate synthase signature 1. / Dihydropteroate synthase / Dihydropteroate synthase domain / Dihydropteroate synthase signature 2. / Dihydropteroate synthase-like / Pterin-binding domain / Pterin binding enzyme / Pterin-binding domain profile. / Dihydropteroate synthase-like / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
2,6-diamino-5-nitropyrimidin-4(3H)-one / : / Dihydropteroate synthase
Similarity search - Component
Biological speciesBacillus anthracis str. A2012 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsYun, M.-K. / White, S.W.
CitationJournal: J.Med.Chem. / Year: 2010
Title: Structural studies of pterin-based inhibitors of dihydropteroate synthase.
Authors: Hevener, K.E. / Yun, M.K. / Qi, J. / Kerr, I.D. / Babaoglu, K. / Hurdle, J.G. / Balakrishna, K. / White, S.W. / Lee, R.E.
History
DepositionApr 14, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Dihydropteroate synthase
B: Dihydropteroate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,78211
Polymers65,7672
Non-polymers1,0159
Water1,892105
1
A: Dihydropteroate synthase
hetero molecules

A: Dihydropteroate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,68610
Polymers65,7672
Non-polymers9198
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_475-x-1,-y+2,z1
Buried area3430 Å2
ΔGint-80 kcal/mol
Surface area20980 Å2
MethodPISA
2
B: Dihydropteroate synthase
hetero molecules

B: Dihydropteroate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,87812
Polymers65,7672
Non-polymers1,11110
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_465-x-1,-y+1,z1
Buried area3730 Å2
ΔGint-100 kcal/mol
Surface area23530 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.513, 97.513, 261.643
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number180
Space group name H-MP6222

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Components

#1: Protein Dihydropteroate synthase


Mass: 32883.734 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus anthracis str. A2012 (bacteria)
Gene: folP, BAO_0074 / Plasmid: PET-28A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: B1UXN2, UniProt: Q81VW8*PLUS, dihydropteroate synthase
#2: Chemical ChemComp-B57 / 2,6-diamino-5-nitropyrimidin-4(3H)-one


Mass: 171.114 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H5N5O3
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 105 / 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: 2.73 Å3/Da / Density % sol: 54.95 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 9
Details: LITHIUM SULFATE, propane, Bis-Tris, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Dec 15, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→47.93 Å / Num. obs: 27556 / % possible obs: 90.2 % / Redundancy: 11.1 % / Rsym value: 0.087 / Net I/σ(I): 33.9
Reflection shellResolution: 2.4→2.49 Å / Redundancy: 8.7 % / Mean I/σ(I) obs: 11.5 / Num. unique all: 1608 / Rsym value: 0.171 / % possible all: 54.1

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Processing

Software
NameVersionClassification
SERGUIControldata collection
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1TX0

1tx0


Resolution: 2.4→47.93 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.918 / SU B: 19.793 / SU ML: 0.224 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.404 / ESU R Free: 0.288 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.28037 1354 5 %RANDOM
Rwork0.22543 ---
obs0.22801 27230 91.52 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 58.905 Å2
Baniso -1Baniso -2Baniso -3
1-3.64 Å21.82 Å20 Å2
2--3.64 Å20 Å2
3----5.46 Å2
Refinement stepCycle: LAST / Resolution: 2.4→47.93 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4139 0 59 105 4303
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0224286
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3021.9835793
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.5425539
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.77825.081185
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.78715777
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.5371523
X-RAY DIFFRACTIONr_chiral_restr0.0870.2651
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.023159
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2040.22080
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.30.22935
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1280.2188
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2750.2109
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1280.24
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.7161.52754
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.03224303
X-RAY DIFFRACTIONr_scbond_it1.6531739
X-RAY DIFFRACTIONr_scangle_it2.5444.51488
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.358 55 -
Rwork0.261 1122 -
obs-1177 55.03 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.8005-0.07130.01991.45220.0793.6204-0.0293-0.1203-0.09530.083-0.036-0.25160.11760.88230.06530.10410.2058-0.016-0.16980.0613-0.2722-78.71179.86190.786
21.54090.00080.21562.4215-0.01973.0530.01770.01290.3152-0.1718-0.1453-0.0702-0.83090.31370.1276-0.03190.2027-0.02130.01370.0545-0.2542-68.41661.043139.108
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 274
2X-RAY DIFFRACTION2B-16 - 274

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