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- PDB-8ok0: Crystal structure of human NQO1 in complex with the inhibitor PMSF -

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Basic information

Entry
Database: PDB / ID: 8ok0
TitleCrystal structure of human NQO1 in complex with the inhibitor PMSF
ComponentsNAD(P)H dehydrogenase [quinone] 1
KeywordsFLAVOPROTEIN / Human NQO1 / flavoenzyme / cancer / inhibitors / PMSF
Function / homology
Function and homology information


response to L-glutamine / response to flavonoid / ubiquinone metabolic process / vitamin E metabolic process / vitamin K metabolic process / NADPH dehydrogenase (quinone) activity / NAD(P)H dehydrogenase (quinone) / cellular response to metal ion / NADH oxidation / cytochrome-b5 reductase activity, acting on NAD(P)H ...response to L-glutamine / response to flavonoid / ubiquinone metabolic process / vitamin E metabolic process / vitamin K metabolic process / NADPH dehydrogenase (quinone) activity / NAD(P)H dehydrogenase (quinone) / cellular response to metal ion / NADH oxidation / cytochrome-b5 reductase activity, acting on NAD(P)H / NADPH oxidation / response to tetrachloromethane / NADH:ubiquinone reductase (non-electrogenic) activity / NAD(P)H dehydrogenase (quinone) activity / response to hydrogen sulfide / response to alkaloid / response to carbohydrate / synaptic transmission, cholinergic / Regulation of ornithine decarboxylase (ODC) / NFE2L2 regulating anti-oxidant/detoxification enzymes / response to testosterone / response to amine / superoxide dismutase activity / response to electrical stimulus / nitric oxide biosynthetic process / removal of superoxide radicals / xenobiotic metabolic process / response to nutrient / cell redox homeostasis / response to hormone / response to ischemia / protein catabolic process / negative regulation of protein catabolic process / response to toxic substance / cellular response to hydrogen peroxide / protein polyubiquitination / positive regulation of neuron apoptotic process / response to estradiol / cellular response to oxidative stress / response to ethanol / response to oxidative stress / response to lipopolysaccharide / innate immune response / neuronal cell body / synapse / dendrite / negative regulation of apoptotic process / RNA binding / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Flavodoxin-like fold / Flavodoxin-like fold / Flavoprotein-like superfamily
Similarity search - Domain/homology
ACETYL GROUP / FLAVIN-ADENINE DINUCLEOTIDE / phenylmethanesulfonic acid / NAD(P)H dehydrogenase [quinone] 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsMartin-Garcia, J.M. / Grieco, A. / Ruiz-Fresneda, M.A.
Funding support Spain, 1items
OrganizationGrant numberCountry
Comunidad de Madrid2019-T1/BMD/15552 Spain
CitationJournal: Febs Lett. / Year: 2023
Title: Structural dynamics at the active site of the cancer-associated flavoenzyme NQO1 probed by chemical modification with PMSF.
Authors: Grieco, A. / Ruiz-Fresneda, M.A. / Gomez-Mulas, A. / Pacheco-Garcia, J.L. / Quereda-Moraleda, I. / Pey, A.L. / Martin-Garcia, J.M.
History
DepositionMar 26, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 1, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 8, 2023Group: Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 22, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NAD(P)H dehydrogenase [quinone] 1
D: NAD(P)H dehydrogenase [quinone] 1
B: NAD(P)H dehydrogenase [quinone] 1
C: NAD(P)H dehydrogenase [quinone] 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,80222
Polymers123,1144
Non-polymers4,68818
Water18,3031016
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22760 Å2
ΔGint-80 kcal/mol
Surface area39000 Å2
Unit cell
Length a, b, c (Å)107.172, 58.928, 189.161
Angle α, β, γ (deg.)90.00, 98.93, 90.00
Int Tables number5
Space group name H-MI121
Components on special symmetry positions
IDModelComponents
11C-548-

HOH

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Components

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Protein , 1 types, 4 molecules ADBC

#1: Protein
NAD(P)H dehydrogenase [quinone] 1


Mass: 30778.432 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: The sequence is correct and the FAD, PMS, GOL and ACE, belong to HETATM and should not be included in the sequence of the protein. So the system is doing something wrong.
Source: (gene. exp.) Homo sapiens (human) / Gene: NQO1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P15559

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Non-polymers , 5 types, 1034 molecules

#2: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
#3: Chemical
ChemComp-PMS / phenylmethanesulfonic acid


Mass: 172.202 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C7H8O3S
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-ACE / ACETYL GROUP


Mass: 44.053 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H4O
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1016 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.32 Å3/Da / Density % sol: 47.08 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.1 M Tris pH 8.5, 0.2 M Sodium Acetate, 20% polyethylene glycol 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.98 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 13, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.6→49.52 Å / Num. obs: 135910 / % possible obs: 99.5 % / Redundancy: 6.6 % / CC1/2: 0.999 / Net I/σ(I): 11.7
Reflection shellResolution: 1.6→1.64 Å / Num. unique obs: 7104 / CC1/2: 0.076 / % possible all: 94.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0419refinement
Aimlessdata scaling
PDB_EXTRACT3.27data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.6→49.47 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.957 / SU B: 4.413 / SU ML: 0.131 / Cross valid method: THROUGHOUT / ESU R: 0.113 / ESU R Free: 0.112 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24654 15129 10 %RANDOM
Rwork0.20788 ---
obs0.21178 135910 98.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 32.967 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å2-0 Å2
2---0 Å20 Å2
3----0 Å2
Refinement stepCycle: 1 / Resolution: 1.6→49.47 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8913 0 0 1016 9929
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0129345
X-RAY DIFFRACTIONr_bond_other_d0.0030.0168752
X-RAY DIFFRACTIONr_angle_refined_deg1.421.82412679
X-RAY DIFFRACTIONr_angle_other_deg0.531.75820183
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.49851119
X-RAY DIFFRACTIONr_dihedral_angle_2_deg5.995538
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.267101551
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0770.21331
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0210880
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022196
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_it2.9323.3924428
X-RAY DIFFRACTIONr_mcbond_other2.9323.3924427
X-RAY DIFFRACTIONr_mcangle_it4.1676.0875555
X-RAY DIFFRACTIONr_mcangle_other4.1676.0875556
X-RAY DIFFRACTIONr_scbond_it3.6633.7874917
X-RAY DIFFRACTIONr_scbond_other3.6633.7884918
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other5.7796.7677123
X-RAY DIFFRACTIONr_long_range_B_refined8.83933.7311397
X-RAY DIFFRACTIONr_long_range_B_other8.86933.211128
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.6→1.642 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.499 972 -
Rwork0.508 8866 -
obs--87 %

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