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- PDB-1urm: HUMAN PEROXIREDOXIN 5, C47S MUTANT -

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Basic information

Entry
Database: PDB / ID: 1urm
TitleHUMAN PEROXIREDOXIN 5, C47S MUTANT
ComponentsPEROXIREDOXIN 5
KeywordsANTIOXIDANT ENZYME / PEROXIREDOXIN / THIOREDOXIN PEROXIDASE / THIOREDOXIN FOLD
Function / homology
Function and homology information


peroxynitrite reductase activity / reactive nitrogen species metabolic process / negative regulation of oxidoreductase activity / negative regulation of transcription by RNA polymerase III / regulation of apoptosis involved in tissue homeostasis / RNA polymerase III transcription regulatory region sequence-specific DNA binding / thioredoxin-dependent peroxiredoxin / thioredoxin peroxidase activity / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / Detoxification of Reactive Oxygen Species ...peroxynitrite reductase activity / reactive nitrogen species metabolic process / negative regulation of oxidoreductase activity / negative regulation of transcription by RNA polymerase III / regulation of apoptosis involved in tissue homeostasis / RNA polymerase III transcription regulatory region sequence-specific DNA binding / thioredoxin-dependent peroxiredoxin / thioredoxin peroxidase activity / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / Detoxification of Reactive Oxygen Species / antioxidant activity / peroxisomal matrix / positive regulation of collagen biosynthetic process / cell redox homeostasis / cellular response to reactive oxygen species / hydrogen peroxide catabolic process / TP53 Regulates Metabolic Genes / peroxidase activity / peroxisome / cellular response to oxidative stress / response to oxidative stress / cytoplasmic vesicle / mitochondrial matrix / inflammatory response / signaling receptor binding / intracellular membrane-bounded organelle / negative regulation of apoptotic process / perinuclear region of cytoplasm / mitochondrion / extracellular space / extracellular exosome / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Peroxiredoxin-5-like / Redoxin / Redoxin / Thioredoxin domain profile. / Thioredoxin domain / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
BENZOIC ACID / Peroxiredoxin-5, mitochondrial
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsDeclercq, J.P. / Evrard, C.
Citation
Journal: J. Chem. Cryst. / Year: 2004
Title: Crystal Structure of the C47S Mutant of Human Peroxiredoxin 5
Authors: Evrard, C. / Smeets, A. / Knoops, B. / Declercq, J.P.
#1: Journal: J.Mol.Biol. / Year: 2001
Title: Crystal Structure of Human Peroxiredoxin 5, a Novel Type of Mammalian Peroxiredoxin at 1.5 A Resolution
Authors: Declercq, J.P. / Evrard, C. / Clippe, A. / Vanderstricht, D. / Bernard, A. / Knoops, B.
#2: Journal: Acta Crystallogr.,Sect.D / Year: 2001
Title: A Twinned Monoclinic Crystal Form of Human Peroxiredoxin 5 with Eight Molecules in the Asymmetric Unit
Authors: Declercq, J.P. / Evrard, C.
#3: Journal: J.Biol.Chem. / Year: 1999
Title: Cloning and Characterization of Aoeb166, a Novel Mammalian Antioxidant Enzyme of the Peroxiredoxin Family
Authors: Knoops, B. / Clippe, A. / Bogard, C. / Arsalane, K. / Wattiez, R. / Hermans, C. / Duconseille, E. / Falmagne, P. / Bernard, A.
History
DepositionOct 31, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 29, 2004Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jul 24, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PEROXIREDOXIN 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,4065
Polymers18,1781
Non-polymers2284
Water5,134285
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)65.646, 65.646, 122.043
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11A-2073-

HOH

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Components

#1: Protein PEROXIREDOXIN 5 / PRX-V / PEROXISOMAL ANTIOXIDANT ENZYME / PLP / THIOREDOXIN PEROXIDASE PMP20 / ANTIOXIDANT ENZYME ...PRX-V / PEROXISOMAL ANTIOXIDANT ENZYME / PLP / THIOREDOXIN PEROXIDASE PMP20 / ANTIOXIDANT ENZYME B166 / AOEB166 / TPX TYPE VI / ALU CO-REPRESSOR 1


Mass: 18177.785 Da / Num. of mol.: 1 / Fragment: RESIDUES 54-214 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: MUTATION CYS 47 SER IN COORDINATES / Source: (gene. exp.) HOMO SAPIENS (human) / Organ: LUNG / Plasmid: PQE-30 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): M15 / References: UniProt: P30044
#2: Chemical ChemComp-BEZ / BENZOIC ACID


Mass: 122.121 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H6O2
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 285 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED MUTATION CYS 100 SER (FOLLOWING NUMBERING OF THE SWISSPROT DATABASE REFERENCE). FUNCTION ...ENGINEERED MUTATION CYS 100 SER (FOLLOWING NUMBERING OF THE SWISSPROT DATABASE REFERENCE). FUNCTION REDUCES HYDROGEN PEROXIDE AND HYDROPEROXIDES WITH REDUCING EQUIVALENTS USING THE THIOREDOXIN SYSTEM.
Sequence detailsC47S MUTANT

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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: 3.4 Å3/Da / Density % sol: 63.5 %
Crystal growpH: 5.3
Details: PROTEIN WAS CRYSTALLIZED FROM 1.6 M AMMONIUM SULFATE, 0.1 M SODIUM CITRATE BUFFER PH 5.3, 0.2 M POTASSIUM SODIUM TARTRATE, 1 MM DTT, 0.02 % (W/V) SODIUM AZIDE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7A / Wavelength: 0.9911
DetectorType: MARRESEARCH / Detector: CCD / Date: Nov 12, 2001 / Details: BENT MIRROR
RadiationMonochromator: DOUBLE CRYSTAL FOCUSING MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9911 Å / Relative weight: 1
ReflectionResolution: 1.7→37 Å / Num. obs: 30149 / % possible obs: 99.8 % / Redundancy: 6.1 % / Rmerge(I) obs: 0.053 / Net I/σ(I): 32
Reflection shellResolution: 1.7→1.74 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.292 / Mean I/σ(I) obs: 5.5 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1HD2

1hd2


Resolution: 1.7→40 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.967 / SU B: 1.189 / SU ML: 0.04 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.067 / ESU R Free: 0.068 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.169 1527 5.1 %RANDOM
Rwork0.146 ---
obs0.147 28558 99.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 15.15 Å2
Baniso -1Baniso -2Baniso -3
1-0.47 Å20 Å20 Å2
2--0.47 Å20 Å2
3----0.93 Å2
Refinement stepCycle: LAST / Resolution: 1.7→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1196 0 12 285 1493
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.0221278
X-RAY DIFFRACTIONr_bond_other_d0.0030.021194
X-RAY DIFFRACTIONr_angle_refined_deg1.631.9861729
X-RAY DIFFRACTIONr_angle_other_deg0.84232808
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9135161
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.1080.2202
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.021409
X-RAY DIFFRACTIONr_gen_planes_other0.0110.02226
X-RAY DIFFRACTIONr_nbd_refined0.2190.2330
X-RAY DIFFRACTIONr_nbd_other0.260.21668
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other0.0930.2921
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1570.2235
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1430.214
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2130.243
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1570.229
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.8221.5814
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.4921316
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.4373464
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.0454.5413
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.7→1.74 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.171 120
Rwork0.179 2072
Refinement TLS params.Method: refined / Origin x: 7.777 Å / Origin y: 41.807 Å / Origin z: 20.122 Å
111213212223313233
T0.0294 Å2-0.006 Å2-0.0071 Å2-0.0316 Å2-0.0164 Å2--0.013 Å2
L0.7648 °20.0261 °20.0285 °2-1.3727 °20.6693 °2--1.4383 °2
S-0.0464 Å °0.0983 Å °-0.0215 Å °-0.1138 Å °-0.0462 Å °0.0957 Å °0.0458 Å °-0.1566 Å °0.0926 Å °

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