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- PDB-6rr6: Structure of 100% reduced KpDyP -

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Basic information

Entry
Database: PDB / ID: 6rr6
TitleStructure of 100% reduced KpDyP
ComponentsIron-dependent peroxidase
KeywordsOXIDOREDUCTASE / heme protein
Function / homology
Function and homology information


Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / peroxidase activity / heme binding / metal ion binding
Similarity search - Function
: / : / Dyp-type peroxidase, C-terminal / Dyp-type peroxidase, N-terminal / DyP-type peroxidase family. / Dyp-type peroxidase / Dimeric alpha-beta barrel
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Peroxidase
Similarity search - Component
Biological speciesKlebsiella pneumoniae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsPfanzagl, V. / Beale, J. / Hofbauer, S.
CitationJournal: J.Biol.Chem. / Year: 2020
Title: X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.
Authors: Pfanzagl, V. / Beale, J.H. / Michlits, H. / Schmidt, D. / Gabler, T. / Obinger, C. / Djinovic-Carugo, K. / Hofbauer, S.
History
DepositionMay 17, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 2, 2020Provider: repository / Type: Initial release
Revision 1.1Oct 7, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / refine
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine.pdbx_diffrn_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Iron-dependent peroxidase
B: Iron-dependent peroxidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,11016
Polymers66,9072
Non-polymers2,20314
Water11,187621
1
A: Iron-dependent peroxidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,6479
Polymers33,4541
Non-polymers1,1938
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Iron-dependent peroxidase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,4637
Polymers33,4541
Non-polymers1,0096
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)50.889, 76.647, 76.579
Angle α, β, γ (deg.)90.00, 108.01, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Iron-dependent peroxidase / Peroxidase / Putative deferrochelatase/peroxidase YfeX


Mass: 33453.605 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Klebsiella pneumoniae (bacteria)
Gene: yfeX, AGG09_21550, B1727_13990, B8011_07420, BL102_0001560, BN49_3985, BVX91_12125, CEO55_07245, CIT28_09840, CP905_14695, PMK1_00271, SAMEA3531778_01640, SM57_03027
Production host: Escherichia coli (E. coli)
References: UniProt: A0A0W8ATM9, Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 621 / 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: 2.12 Å3/Da / Density % sol: 42.06 %
Crystal growMethod: vapor diffusion, sitting drop / pH: 8.5
Details: 23% w/v PEG 3350, 0.1 M MgCl2, 0.1 M Tris-HCl, pH 8.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 16, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.9→47.67 Å / Num. obs: 43552 / % possible obs: 98.7 % / Redundancy: 5.4 % / Biso Wilson estimate: 11.56 Å2 / Net I/σ(I): 6
Reflection shellResolution: 1.9→1.91 Å / Num. unique obs: 2789

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Processing

Software
NameVersionClassification
BUSTER2.10.3refinement
XDSdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6FKS

6fks


Resolution: 1.9→47.67 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.897 / SU R Cruickshank DPI: 0.578 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.191 / SU Rfree Blow DPI: 0.139 / SU Rfree Cruickshank DPI: 0.136
RfactorNum. reflection% reflectionSelection details
Rfree0.199 978 2.25 %RANDOM
Rwork0.181 ---
obs0.182 43521 98.5 %-
Displacement parametersBiso mean: 12.01 Å2
Baniso -1Baniso -2Baniso -3
1-2.0036 Å20 Å21.0169 Å2
2---2.4006 Å20 Å2
3---0.397 Å2
Refine analyzeLuzzati coordinate error obs: 0.22 Å
Refinement stepCycle: 1 / Resolution: 1.9→47.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4662 0 148 621 5431
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0179869HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.3617784HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d2174SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes1636HARMONIC5
X-RAY DIFFRACTIONt_it9869HARMONIC20
X-RAY DIFFRACTIONt_nbd10SEMIHARMONIC5
X-RAY DIFFRACTIONt_omega_torsion3.71
X-RAY DIFFRACTIONt_other_torsion16.04
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion605SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact10823SEMIHARMONIC4
LS refinement shellResolution: 1.9→1.91 Å / Total num. of bins used: 48
RfactorNum. reflection% reflection
Rfree0.2561 -2.21 %
Rwork0.2506 887 -
all0.2507 907 -
obs--98 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.40420.3357-0.05680.1046-0.106-0.07970.01520.01780.0387-0.022-0.01280.03430.0322-0.0013-0.0024-0.0479-0.001-0.0102-0.02470.0009-0.033214.20192.0054-2.1586
20.11720.1874-0.03290-0.0341-0.0338-0.01980.00220.0192-0.01140.01180.00280.01890.00240.0079-0.04680.0082-0.01560.0012-0.0086-0.044524.74490.401332.7265
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|* }
2X-RAY DIFFRACTION2{ B|* }

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