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- PDB-7wy4: Structure of the CYP102A1 F87A Haem Domain with N-Enanthyl-L-Prol... -

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Basic information

Entry
Database: PDB / ID: 7wy4
TitleStructure of the CYP102A1 F87A Haem Domain with N-Enanthyl-L-Prolyl-L-Phenylalanine in complex with Styrene
ComponentsBifunctional cytochrome P450/NADPH--P450 reductase
KeywordsOXIDOREDUCTASE / Monooxygenase
Function / homology
Function and homology information


NADPH-hemoprotein reductase / NADPH-hemoprotein reductase activity / unspecific monooxygenase / aromatase activity / response to hormone / FMN binding / flavin adenine dinucleotide binding / iron ion binding / heme binding / cytosol
Similarity search - Function
Bifunctional cytochrome P450/NADPH--cytochrome P450 reductase / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / FAD binding domain / Flavodoxin-like / Flavoprotein pyridine nucleotide cytochrome reductase / Flavodoxin / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Oxidoreductase FAD/NAD(P)-binding ...Bifunctional cytochrome P450/NADPH--cytochrome P450 reductase / Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding / NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily / FAD binding domain / Flavodoxin-like / Flavoprotein pyridine nucleotide cytochrome reductase / Flavodoxin / Flavodoxin-like domain profile. / Flavodoxin/nitric oxide synthase / Oxidoreductase FAD/NAD(P)-binding / Oxidoreductase NAD-binding domain / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Ferredoxin reductase-type FAD binding domain profile. / Riboflavin synthase-like beta-barrel / Cytochrome P450, conserved site / Cytochrome P450 cysteine heme-iron ligand signature. / Flavoprotein-like superfamily / Cytochrome P450 / Cytochrome P450 superfamily / Cytochrome P450
Similarity search - Domain/homology
Chem-D0L / PROTOPORPHYRIN IX CONTAINING FE / ethenylbenzene / Bifunctional cytochrome P450/NADPH--P450 reductase
Similarity search - Component
Biological speciesPriestia megaterium (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å
AuthorsSuzuki, K. / Stanfield, J.K. / Shisaka, Y. / Omura, K. / Kasai, C. / Sugimoto, H. / Shoji, O.
Funding support Japan, 4items
OrganizationGrant numberCountry
Japan Science and TechnologyJPMJCR15P3 Japan
Japan Society for the Promotion of Science (JSPS)JP15H05806 Japan
Japan Society for the Promotion of Science (JSPS)JP18J23340 Japan
Japan Society for the Promotion of Science (JSPS)JP18J15250 Japan
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2023
Title: A Compound I Mimic Reveals the Transient Active Species of a Cytochrome P450 Enzyme: Insight into the Stereoselectivity of P450-Catalysed Oxidations.
Authors: Suzuki, K. / Stanfield, J.K. / Omura, K. / Shisaka, Y. / Ariyasu, S. / Kasai, C. / Aiba, Y. / Sugimoto, H. / Shoji, O.
History
DepositionFeb 15, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 4, 2023Provider: repository / Type: Initial release
Revision 1.1Feb 15, 2023Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.2Mar 29, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _citation_author.identifier_ORCID
Revision 1.3May 3, 2023Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.4Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Bifunctional cytochrome P450/NADPH--P450 reductase
B: Bifunctional cytochrome P450/NADPH--P450 reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)108,43229
Polymers104,4492
Non-polymers3,98327
Water15,763875
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A: Bifunctional cytochrome P450/NADPH--P450 reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,26215
Polymers52,2251
Non-polymers2,03814
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area19450 Å2
MethodPISA
2
B: Bifunctional cytochrome P450/NADPH--P450 reductase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,17014
Polymers52,2251
Non-polymers1,94513
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1320 Å2
ΔGint-22 kcal/mol
Surface area19050 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.970, 126.650, 148.750
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Bifunctional cytochrome P450/NADPH--P450 reductase


Mass: 52224.562 Da / Num. of mol.: 2 / Mutation: F87A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Priestia megaterium (bacteria) / Gene: BTA37_15100 / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: A0A1Q8UP87, unspecific monooxygenase, NADPH-hemoprotein reductase

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Non-polymers , 6 types, 902 molecules

#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-D0L / (2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid


Mass: 360.490 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H32N2O3
#4: Chemical ChemComp-SYN / ethenylbenzene / styrene


Mass: 104.149 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H8
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#6: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: C3H8O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 875 / 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: 2.66 Å3/Da / Density % sol: 53.74 %
Crystal growTemperature: 293 K / Method: batch mode / Details: PEG8000, Magnesium Chloride, Tris-HCl

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL45XU / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 X 6M / Detector: PIXEL / Date: Jul 13, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.45→48.22 Å / Num. obs: 187448 / % possible obs: 100 % / Redundancy: 6.761 % / Biso Wilson estimate: 24.687 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.113 / Rrim(I) all: 0.122 / Χ2: 0.869 / Net I/σ(I): 9.74 / Num. measured all: 2579772 / Scaling rejects: 159
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.45-1.496.2631.6771.2717736128341283190.6341.8399.9
1.49-1.536.8631.3161.7618846427484274600.7711.42399.9
1.53-1.576.9291.0442.2718569026807267980.8571.128100
1.57-1.626.8590.8172.8817822025995259840.9070.884100
1.62-1.676.7430.6883.4216981625187251850.9280.745100
1.67-1.736.3740.5284.2415561424423244150.9470.576100
1.73-1.86.7570.4485.3315849923464234560.9680.485100
1.8-1.877.080.3526.8516043722661226610.9830.379100
1.87-1.967.0630.2818.4815341821728217220.9890.303100
1.96-2.056.9960.21510.4814493720717207160.9920.232100
2.05-2.166.6520.16412.313095119688196850.9940.178100
2.16-2.296.7260.12814.5412576518701186990.9950.139100
2.29-2.457.2240.10816.6112651017514175120.9970.116100
2.45-2.657.0790.09218.4111540816304163040.9970.1100
2.65-2.96.840.07920.0810253014991149900.9970.085100
2.9-3.246.1140.06721.378290913576135610.9970.07499.9
3.24-3.746.8450.0626.228193911972119700.9980.064100
3.74-4.596.5190.05627.886585310103101010.9980.061100
4.59-6.485.8790.05526.4545811780377920.9980.0699.9
6.48-48.226.9640.04730.5329640426842560.9990.0599.7

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Processing

Software
NameVersionClassification
XSCALEdata scaling
REFMAC5.8.0257refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3WSP

3wsp


Resolution: 1.45→48.22 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.971 / SU B: 2.634 / SU ML: 0.043 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.068 / ESU R Free: 0.061 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1792 9838 5 %RANDOM
Rwork0.1433 ---
obs0.1451 187448 99.97 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 75.89 Å2 / Biso mean: 19.671 Å2 / Biso min: 7.26 Å2
Baniso -1Baniso -2Baniso -3
1--0.7 Å2-0 Å20 Å2
2--1.18 Å2-0 Å2
3----0.48 Å2
Refinement stepCycle: final / Resolution: 1.45→48.22 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7316 0 420 875 8611
Biso mean--25.65 30.99 -
Num. residues----908
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0139394
X-RAY DIFFRACTIONr_bond_other_d0.0010.0178677
X-RAY DIFFRACTIONr_angle_refined_deg1.5271.69412846
X-RAY DIFFRACTIONr_angle_other_deg1.4331.61920306
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.59751173
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.4423.664494
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.93151668
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.0141549
X-RAY DIFFRACTIONr_chiral_restr0.0840.21141
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0210828
X-RAY DIFFRACTIONr_gen_planes_other0.0040.021946
X-RAY DIFFRACTIONr_rigid_bond_restr1.492318071
LS refinement shellResolution: 1.45→1.488 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.332 749 -
Rwork0.325 13723 -
all-14472 -
obs--99.95 %

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