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- PDB-7daz: Crystal structure of Drosophila melanogaster Noppera-bo, glutathi... -

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Basic information

Entry
Database: PDB / ID: 7daz
TitleCrystal structure of Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14), in TDP015- and GSH-bound form
ComponentsGlutathione S-transferase E14
KeywordsTRANSFERASE / Drosophila melanogaster / Glutathione S-transferase / GST / GSTE14 / Inhibitor / Ecdysteroid
Function / homology
Function and homology information


ecdysteroid biosynthetic process / steroid Delta-isomerase activity / glutathione transferase / glutathione transferase activity / glutathione metabolic process / cholesterol homeostasis / response to toxic substance / cytoplasm
Similarity search - Function
Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Thioredoxin-like superfamily
Similarity search - Domain/homology
GLUTATHIONE / Chem-H29 / Glutathione S-transferase E14
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.64 Å
AuthorsKoiwai, K. / Inaba, K. / Yumoto, F. / Senda, T. / Niwa, R.
Funding support Japan, 3items
OrganizationGrant numberCountry
Japan Agency for Medical Research and Development (AMED)18am0101113j0002 Japan
Japan Society for the Promotion of Science (JSPS)15K14719 Japan
Japan Society for the Promotion of Science (JSPS)18K19163 Japan
CitationJournal: J Pestic Sci / Year: 2021
Title: Non-steroidal inhibitors of Drosophila melanogaster steroidogenic glutathione S -transferase Noppera-bo
Authors: Koiwai, K. / Morohashi, K. / Inaba, K. / Ebihara, K. / Kojima, H. / Okabe, T. / Yoshino, R. / Hirokawa, T. / Nampo, T. / Fujikawa, Y. / Inoue, H. / Yumoto, F. / Senda, T. / Niwa, R.
History
DepositionOct 18, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 10, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 31, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Nov 29, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model
Item: _citation.country / _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: Glutathione S-transferase E14
B: Glutathione S-transferase E14
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,6278
Polymers55,0882
Non-polymers1,5406
Water5,711317
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4220 Å2
ΔGint-29 kcal/mol
Surface area17780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.333, 75.959, 111.147
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Glutathione S-transferase E14 / Protein noppera-bo


Mass: 27543.766 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: GstE14, GSTD14-14, nobo, CG4688 / Plasmid: pCOLD III / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q7JYX0, glutathione transferase
#2: Chemical ChemComp-GSH / GLUTATHIONE


Mass: 307.323 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H17N3O6S / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-H29 / 6-(6,7-dihydro-4H-thieno[3,2-c]pyridin-5-yl)pyridin-3-amine


Mass: 231.317 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: C12H13N3S / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 317 / 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: 2.42 Å3/Da / Density % sol: 49.18 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.4 / Details: 34% (v/v) PPG 400 in 80mM Bis-Tris, pH 6.4

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: TPS 05A / Wavelength: 0.98 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Aug 16, 2018
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.64→35.94 Å / Num. obs: 61231 / % possible obs: 1 % / Observed criterion σ(I): 2 / Redundancy: 14.4 % / Biso Wilson estimate: 29.67 Å2 / CC1/2: 1 / CC star: 1 / Rmerge(I) obs: 0.055 / Rrim(I) all: 0.057 / Net I/σ(I): 23.98
Reflection shellResolution: 1.64→1.699 Å / Redundancy: 14.7 % / Rmerge(I) obs: 1.221 / Mean I/σ(I) obs: 2.14 / Num. unique obs: 6042 / CC1/2: 0.861 / CC star: 0.962 / Rrim(I) all: 1.265 / % possible all: 1

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Processing

Software
NameVersionClassification
PHENIX(1.18.2_3874)refinement
XDSJun 17, 2015data reduction
Aimless0.5.15data scaling
MOLREP11.7.02phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6KEM

6kem


Resolution: 1.64→35.94 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.67 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2218 3079 5.04 %
Rwork0.1919 --
obs0.1934 61094 99.72 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.64→35.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3528 0 104 317 3949
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0053865
X-RAY DIFFRACTIONf_angle_d1.2175259
X-RAY DIFFRACTIONf_dihedral_angle_d17.9541428
X-RAY DIFFRACTIONf_chiral_restr0.22574
X-RAY DIFFRACTIONf_plane_restr0.004688
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.64-1.670.3291510.30492627X-RAY DIFFRACTION100
1.67-1.690.37731340.2952597X-RAY DIFFRACTION100
1.69-1.720.33681380.28492608X-RAY DIFFRACTION100
1.72-1.750.27091330.27572606X-RAY DIFFRACTION100
1.75-1.790.30231360.26672605X-RAY DIFFRACTION100
1.79-1.820.30441280.2512648X-RAY DIFFRACTION100
1.82-1.860.28241470.25732580X-RAY DIFFRACTION100
1.86-1.910.32141440.27042560X-RAY DIFFRACTION98
1.91-1.950.27511380.26832597X-RAY DIFFRACTION98
1.95-2.010.26231380.22372617X-RAY DIFFRACTION100
2.01-2.070.23361510.21942607X-RAY DIFFRACTION100
2.07-2.130.26061330.20872605X-RAY DIFFRACTION100
2.13-2.210.24011610.20552630X-RAY DIFFRACTION100
2.21-2.30.27811110.21962636X-RAY DIFFRACTION99
2.3-2.40.23821320.19712651X-RAY DIFFRACTION100
2.4-2.530.21841500.19872650X-RAY DIFFRACTION100
2.53-2.690.22391600.19962600X-RAY DIFFRACTION100
2.69-2.890.22981350.19472679X-RAY DIFFRACTION100
2.89-3.190.22921390.19532676X-RAY DIFFRACTION100
3.19-3.650.17651430.18112687X-RAY DIFFRACTION100
3.65-4.590.15551360.14532726X-RAY DIFFRACTION100
4.59-35.940.23291410.17172823X-RAY DIFFRACTION99

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