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- PDB-3fmu: Crystal Structure Analysis of Fungal Versatile Peroxidase from Pl... -

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Basic information

Entry
Database: PDB / ID: 3fmu
TitleCrystal Structure Analysis of Fungal Versatile Peroxidase from Pleurotus eryngii
ComponentsVersatile peroxidase VPL2
KeywordsOXIDOREDUCTASE / CLASS II (FUNGAL) PEROXIDASES / protoporphyrin IX / ELECTRON TRANSFER / LIGNIN PEROXIDASE / LIGNIN DEGRADATION / MANGANESE PEROXIDASE / MN-INDEPENDENT OXIDATION PHENOLIC NON-PHENOLIC AROMATICS / MNII OXIDATION / PEROXIDASE / POLYVALENT PEROXIDASE / Heme / Hydrogen peroxide / Iron / Manganese / Metal-binding / Secreted / Zymogen
Function / homology
Function and homology information


versatile peroxidase / reactive-black-5:hydrogen-peroxide oxidoreductase activity / manganese peroxidase activity / lignin catabolic process / response to reactive oxygen species / hydrogen peroxide catabolic process / cellular response to oxidative stress / heme binding / extracellular region / metal ion binding
Similarity search - Function
Fungal ligninase / Fungal ligninase, C-terminal / Fungal peroxidase extension region / Heme-binding peroxidase Ccp1-like / Peroxidase; domain 2 / Peroxidase, domain 2 / Peroxidase; domain 1 - #10 / Peroxidase; domain 1 / Peroxidases heam-ligand binding site / Peroxidase, active site ...Fungal ligninase / Fungal ligninase, C-terminal / Fungal peroxidase extension region / Heme-binding peroxidase Ccp1-like / Peroxidase; domain 2 / Peroxidase, domain 2 / Peroxidase; domain 1 - #10 / Peroxidase; domain 1 / Peroxidases heam-ligand binding site / Peroxidase, active site / Peroxidases active site signature. / Plant heme peroxidase family profile. / Haem peroxidase / Peroxidase / Peroxidases proximal heme-ligand signature. / Haem peroxidase superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
CACODYLATE ION / : / PROTOPORPHYRIN IX CONTAINING FE / Versatile peroxidase VPL2
Similarity search - Component
Biological speciesPleurotus eryngii (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.04 Å
AuthorsPiontek, K. / Martinez, A.T. / Choinowski, T. / Plattner, D.A.
CitationJournal: To be Published
Title: Structural and Site-directed Mutagenesis Study of Versatile Peroxidase Oxidizing both Mn(II) and Aromatic Substrates
Authors: Piontek, K. / Choinowski, T. / Perez-Boada, M. / Ruiz-Duenas, F.J. / Martinez, M.J. / Plattner, D.A. / Martinez, A.T.
History
DepositionDec 22, 2008Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Dec 22, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Nov 10, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 1, 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: Versatile peroxidase VPL2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,14318
Polymers34,5071
Non-polymers1,63617
Water9,440524
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)63.199, 63.199, 99.237
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number78
Space group name H-MP43

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Versatile peroxidase VPL2 / Versatile liquid phase peroxidase 2


Mass: 34506.570 Da / Num. of mol.: 1 / Mutation: W164S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pleurotus eryngii (fungus) / Strain: IJFM, A169 / Gene: VPL2 / Plasmid: PFLAG1-VPL2 / Production host: Escherichia coli (E. coli) / Strain (production host): W3110 / References: UniProt: O94753, versatile peroxidase

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Non-polymers , 6 types, 541 molecules

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


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#5: Chemical
ChemComp-FE / FE (III) ION / Iron


Mass: 55.845 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Fe
#6: Chemical ChemComp-CAC / CACODYLATE ION / dimethylarsinate / Cacodylic acid


Mass: 136.989 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6AsO2
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 524 / 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: 2.87 Å3/Da / Density % sol: 57.17 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5
Details: 9.0mg/ml protein in 10mM Na-tartrate pH 5.5, 14% PEG 8000, 100mM Zn-acetate, 100mM Na-cacodylate pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.891976 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Jun 18, 2003
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.891976 Å / Relative weight: 1
ReflectionResolution: 1.03→80 Å / Num. all: 191427 / Num. obs: 186809 / % possible obs: 97.6 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.98 % / Biso Wilson estimate: 11.4 Å2 / Rmerge(I) obs: 0.108 / Rsym value: 0.097 / Net I/σ(I): 11.95
Reflection shellResolution: 1.03→1.15 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.299 / Mean I/σ(I) obs: 4.57 / Num. unique all: 53827 / Rsym value: 0.254 / % possible all: 91.8

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
AMoREphasing
REFMAC5.2.0019refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3FKG

3fkg


Resolution: 1.04→44.688 Å / Cor.coef. Fo:Fc: 0.981 / Cor.coef. Fo:Fc free: 0.979 / SU B: 0.349 / SU ML: 0.008 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.017 / ESU R Free: 0.017 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.12301 9281 5 %RANDOM
Rwork0.11092 ---
all0.1151 176589 --
obs0.11151 175971 99.65 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 12.107 Å2
Baniso -1Baniso -2Baniso -3
1-0.04 Å20 Å20 Å2
2--0.04 Å20 Å2
3----0.08 Å2
Refinement stepCycle: LAST / Resolution: 1.04→44.688 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2348 0 63 524 2935
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0222588
X-RAY DIFFRACTIONr_bond_other_d0.0010.022386
X-RAY DIFFRACTIONr_angle_refined_deg1.4692.0193536
X-RAY DIFFRACTIONr_angle_other_deg0.77335511
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.025352
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.51725.505109
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.48115384
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8161510
X-RAY DIFFRACTIONr_chiral_restr0.0980.2393
X-RAY DIFFRACTIONr_gen_planes_refined0.010.022990
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02526
X-RAY DIFFRACTIONr_nbd_refined0.2340.3561
X-RAY DIFFRACTIONr_nbd_other0.2220.32562
X-RAY DIFFRACTIONr_nbtor_refined0.1840.51314
X-RAY DIFFRACTIONr_nbtor_other0.0920.51352
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1640.5583
X-RAY DIFFRACTIONr_metal_ion_refined0.0630.26
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1710.39
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3070.338
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1520.556
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined0.0730.22
X-RAY DIFFRACTIONr_mcbond_it2.10621680
X-RAY DIFFRACTIONr_mcbond_other1.5852658
X-RAY DIFFRACTIONr_mcangle_it2.89432667
X-RAY DIFFRACTIONr_scbond_it3.0512985
X-RAY DIFFRACTIONr_scangle_it4.0543850
X-RAY DIFFRACTIONr_rigid_bond_restr1.91532665
X-RAY DIFFRACTIONr_sphericity_free10.4693530
X-RAY DIFFRACTIONr_sphericity_bonded5.03432489
LS refinement shellResolution: 1.04→1.067 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.213 682 -
Rwork0.195 12835 -
obs--98.76 %

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