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- PDB-5ioq: Flavin-dependent thymidylate synthase in complex with FAD and deo... -

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Basic information

Entry
Database: PDB / ID: 5ioq
TitleFlavin-dependent thymidylate synthase in complex with FAD and deoxyuridine
ComponentsThymidylate synthase ThyX
KeywordsTRANSFERASE / FAD-dependent / nucleotide biosynthesis / reductive methylation
Function / homology
Function and homology information


thymidylate synthase (FAD) / thymidylate synthase (FAD) activity / thymidylate synthase activity / dTMP biosynthetic process / dTTP biosynthetic process / NADPH binding / flavin adenine dinucleotide binding / methylation
Similarity search - Function
Gyrase A; domain 2 - #170 / Thymidylate synthase ThyX / Thymidylate synthase ThyX superfamily / Thymidylate synthase complementing protein / Flavin-dependent thymidylate synthase (thyX) domain profile. / Gyrase A; domain 2 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
2'-DEOXYURIDINE / FLAVIN-ADENINE DINUCLEOTIDE / TRIETHYLENE GLYCOL / Flavin-dependent thymidylate synthase
Similarity search - Component
Biological speciesThermotoga maritima (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.93 Å
AuthorsBernard, S.M. / Stull, F.W. / Smith, J.L.
Funding support United States, 3items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)1213620 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01DK042303 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM081544 United States
CitationJournal: Biochemistry / Year: 2016
Title: Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.
Authors: Stull, F.W. / Bernard, S.M. / Sapra, A. / Smith, J.L. / Zuiderweg, E.R. / Palfey, B.A.
History
DepositionMar 8, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 8, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 22, 2016Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Database references / Derived calculations
Category: citation / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Nov 27, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Thymidylate synthase ThyX
B: Thymidylate synthase ThyX
C: Thymidylate synthase ThyX
D: Thymidylate synthase ThyX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)115,57122
Polymers110,0154
Non-polymers5,55718
Water3,351186
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25710 Å2
ΔGint10 kcal/mol
Surface area31700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.190, 116.113, 141.891
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11METMETLEULEUAA1 - 21513 - 227
21METMETLEULEUBB1 - 21513 - 227
12HISHISLEULEUAA0 - 21512 - 227
22HISHISLEULEUCC0 - 21512 - 227
13METMETILEILEAA1 - 21413 - 226
23METMETILEILEDD1 - 21413 - 226
14METMETILEILEBB1 - 21413 - 226
24METMETILEILECC1 - 21413 - 226
15METMETILEILEBB1 - 21413 - 226
25METMETILEILEDD1 - 21413 - 226
16METMETGLNGLNCC1 - 21913 - 231
26METMETGLNGLNDD1 - 21913 - 231

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein
Thymidylate synthase ThyX / TSase


Mass: 27503.680 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) (bacteria)
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / Gene: thyX, thy1, TM_0449 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9WYT0, thymidylate synthase (FAD)
#2: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical
ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C6H14O4
#4: Chemical
ChemComp-DUR / 2'-DEOXYURIDINE / Deoxyuridine


Mass: 228.202 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C9H12N2O5 / Comment: antivirus*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 186 / 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: 2.03 Å3/Da / Density % sol: 39.37 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion / pH: 8
Details: 40-50% PEG 200, 0-150 mM NaCl, 100 mM Tris-HCl pH 8.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.033 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 6, 2013
RadiationMonochromator: double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 1.93→89.86 Å / Num. obs: 67137 / % possible obs: 98.1 % / Redundancy: 7.6 % / Rsym value: 0.094 / Net I/σ(I): 22.8

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Processing

Software
NameVersionClassification
REFMAC5.8.0069refinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4GT9

4gt9


Resolution: 1.93→89.86 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.956 / SU B: 3.598 / SU ML: 0.101 / Cross valid method: THROUGHOUT / ESU R: 0.168 / ESU R Free: 0.141 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2018 3318 5 %RANDOM
Rwork0.17072 ---
obs0.1723 62459 96.17 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 39.126 Å2
Baniso -1Baniso -2Baniso -3
1-1.3 Å20 Å2-0 Å2
2---1 Å20 Å2
3----0.3 Å2
Refinement stepCycle: 1 / Resolution: 1.93→89.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7142 0 367 186 7695
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0197740
X-RAY DIFFRACTIONr_bond_other_d0.0050.027303
X-RAY DIFFRACTIONr_angle_refined_deg1.4751.99810475
X-RAY DIFFRACTIONr_angle_other_deg1.121316754
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8325847
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.94522.293375
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.656151287
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.91570
X-RAY DIFFRACTIONr_chiral_restr0.090.21100
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0218296
X-RAY DIFFRACTIONr_gen_planes_other0.0050.021906
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_it2.6563.5763406
X-RAY DIFFRACTIONr_mcbond_other2.6553.5753405
X-RAY DIFFRACTIONr_mcangle_it3.8215.344247
X-RAY DIFFRACTIONr_mcangle_other3.8215.3414248
X-RAY DIFFRACTIONr_scbond_it3.4874.0624334
X-RAY DIFFRACTIONr_scbond_other3.4874.0624334
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other5.6265.8866229
X-RAY DIFFRACTIONr_long_range_B_refined7.28829.8329315
X-RAY DIFFRACTIONr_long_range_B_other7.28829.8329315
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A131390.09
12B131390.09
21A130220.1
22C130220.1
31A130000.09
32D130000.09
41B131760.07
42C131760.07
51B131090.08
52D131090.08
61C135350.08
62D135350.08
LS refinement shellResolution: 1.928→1.978 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.295 177 -
Rwork0.257 3340 -
obs--70.64 %

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