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- PDB-8rnm: Unspecific peroxygenase from Marasmius wettsteinii (MweUPO-1) in ... -

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Basic information

Entry
Database: PDB / ID: 8rnm
TitleUnspecific peroxygenase from Marasmius wettsteinii (MweUPO-1) in complex with testosterone
ComponentsUnspecific peroxygenase
KeywordsOXIDOREDUCTASE / Peroxygenase / peroxidase / complex / testosterone
Function / homologyPROTOPORPHYRIN IX CONTAINING FE / DI(HYDROXYETHYL)ETHER / TESTOSTERONE
Function and homology information
Biological speciesMarasmius wettsteinii (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsFernandez-Garcia, A. / Sanz-Aparicio, J.
Funding support Spain, 1items
OrganizationGrant numberCountry
Spanish Ministry of Science, Innovation, and UniversitiesSynergy CAM Project Y2018/BIO-4738-EVOQUIMERA-CM Spain
CitationJournal: Acs Chem.Biol. / Year: 2024
Title: Structural Insights and Reaction Profile of a New Unspecific Peroxygenase from Marasmius wettsteinii Produced in a Tandem-Yeast Expression System.
Authors: Sanchez-Moreno, I. / Fernandez-Garcia, A. / Mateljak, I. / Gomez de Santos, P. / Hofrichter, M. / Kellner, H. / Sanz-Aparicio, J. / Alcalde, M.
History
DepositionJan 10, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 16, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 30, 2024Group: 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: Unspecific peroxygenase
B: Unspecific peroxygenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,45221
Polymers51,7982
Non-polymers3,65419
Water7,332407
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: PISA-dimeric
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8250 Å2
ΔGint-98 kcal/mol
Surface area20100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)75.999, 75.999, 185.826
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

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Protein / Sugars , 2 types, 6 molecules AB

#1: Protein Unspecific peroxygenase


Mass: 25899.092 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Marasmius wettsteinii (fungus) / Production host: Komagataella phaffii CBS 7435 (fungus) / References: unspecific peroxygenase
#2: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 7 types, 422 molecules

#3: 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
#4: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C4H10O3
#5: Chemical ChemComp-TES / TESTOSTERONE


Mass: 288.424 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H28O2 / Feature type: SUBJECT OF INVESTIGATION / Comment: hormone*YM
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#8: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 407 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 2.43 Å3/Da / Density % sol: 49.33 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop
Details: 13% PEG 4000, 200mM ammonium sulfate. Soaking: 40 mM testosterone, 5 hours, cryoprotected with 15% glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 22, 2021 / Details: KB MIRRORS
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 1.95→48.01 Å / Num. obs: 40573 / % possible obs: 99.7 % / Redundancy: 7.1 % / CC1/2: 0.996 / Rmerge(I) obs: 0.082 / Rpim(I) all: 0.033 / Rrim(I) all: 0.089 / Χ2: 0.98 / Net I/σ(I): 13.2
Reflection shellResolution: 1.95→2 Å / Redundancy: 7.6 % / Rmerge(I) obs: 0.576 / Mean I/σ(I) obs: 2.8 / Num. unique obs: 2816 / CC1/2: 0.084 / Rpim(I) all: 0.221 / Rrim(I) all: 0.618 / Χ2: 0.7 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0403refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.95→40.62 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.94 / SU B: 4.154 / SU ML: 0.115 / Cross valid method: THROUGHOUT / ESU R: 0.177 / ESU R Free: 0.153 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22659 1986 5 %RANDOM
Rwork0.1939 ---
obs0.19555 37917 98.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 29.549 Å2
Baniso -1Baniso -2Baniso -3
1-0.55 Å20 Å20 Å2
2--0.55 Å20 Å2
3----1.1 Å2
Refinement stepCycle: 1 / Resolution: 1.95→40.62 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3642 0 242 407 4291
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0124027
X-RAY DIFFRACTIONr_bond_other_d0.0010.0163752
X-RAY DIFFRACTIONr_angle_refined_deg1.3061.695527
X-RAY DIFFRACTIONr_angle_other_deg0.4651.5918671
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5965494
X-RAY DIFFRACTIONr_dihedral_angle_2_deg7.598529
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.79910604
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0650.2618
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.024709
X-RAY DIFFRACTIONr_gen_planes_other0.0080.02883
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_it2.0093.0541934
X-RAY DIFFRACTIONr_mcbond_other2.0093.0541934
X-RAY DIFFRACTIONr_mcangle_it2.8615.4922418
X-RAY DIFFRACTIONr_mcangle_other2.865.4942419
X-RAY DIFFRACTIONr_scbond_it2.5673.3922093
X-RAY DIFFRACTIONr_scbond_other2.5623.3872082
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.9486.1183084
X-RAY DIFFRACTIONr_long_range_B_refined5.1830.954747
X-RAY DIFFRACTIONr_long_range_B_other5.16330.944652
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.95→2.001 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.297 148 -
Rwork0.252 2801 -
obs--99.9 %

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