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- PDB-2zaw: Crystal Structure of Ferric Cytochrome P450cam Reconstituted with... -

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Basic information

Entry
Database: PDB / ID: 2zaw
TitleCrystal Structure of Ferric Cytochrome P450cam Reconstituted with 6-Methyl-6-depropionated Hemin
ComponentsCytochrome P450-cam
KeywordsOXIDOREDUCTASE / P450CAM / MONOOXYGENASE / CAMPHOR-HYDROXYLASE / Heme / Iron / Membrane / Metal-binding
Function / homology
Function and homology information


camphor 5-monooxygenase / camphor 5-monooxygenase activity / (+)-camphor catabolic process / iron ion binding / heme binding / cytoplasm
Similarity search - Function
Cytochrome P450, B-class / Cytochrome p450 / Cytochrome P450 / Cytochrome P450, conserved site / Cytochrome P450 cysteine heme-iron ligand signature. / Cytochrome P450 / Cytochrome P450 superfamily / Cytochrome P450 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
6-METHY-6-DEPROPIONATEHEMIN / CAMPHOR / : / Camphor 5-monooxygenase
Similarity search - Component
Biological speciesPseudomonas putida (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å
AuthorsHarada, K. / Sakurai, K. / Shimada, H. / Tsukihara, T. / Hayashi, T.
CitationJournal: J.Am.Chem.Soc. / Year: 2008
Title: Evaluation of the functional role of the heme-6-propionate side chain in cytochrome P450cam
Authors: Harada, K. / Sakurai, K. / Ikemura, K. / Ogura, T. / Hirota, S. / Shimada, H. / Hayashi, T.
History
DepositionOct 11, 2007Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 1, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jun 20, 2018Group: Data collection / Experimental preparation / Category: exptl_crystal_grow
Item: _exptl_crystal_grow.pdbx_details / _exptl_crystal_grow.temp
Revision 1.3Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytochrome P450-cam
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,5055
Polymers46,7201
Non-polymers7854
Water14,340796
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)63.675, 63.675, 250.272
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 , 1 types, 1 molecules A

#1: Protein Cytochrome P450-cam / Camphor 5-monooxygenase / P450cam


Mass: 46720.074 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas putida (bacteria) / Gene: camC, cyp101 / Plasmid: M13tv19 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P00183, camphor 5-monooxygenase

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Non-polymers , 5 types, 800 molecules

#2: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-6HE / 6-METHY-6-DEPROPIONATEHEMIN


Mass: 558.451 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C32H30FeN4O2
#5: Chemical ChemComp-CAM / CAMPHOR


Mass: 152.233 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16O
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 796 / 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: 2.71 Å3/Da / Density % sol: 54.69 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: 14% PEG 8000, 50mM Tris-HCl, 250mM KCl, 1mM d-camphor, 10mM dithioerythritol(DTE), pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.7 Å
DetectorType: Bruker DIP-6040 / Detector: CCD / Date: Jun 11, 2007
RadiationMonochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.7 Å / Relative weight: 1
ReflectionResolution: 1.55→45.04 Å / Num. all: 75813 / Num. obs: 75813 / % possible obs: 99.8 % / Redundancy: 7.3 % / Biso Wilson estimate: 13.92 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 9.1
Reflection shellResolution: 1.55→1.59 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.387 / Mean I/σ(I) obs: 5.9 / Num. unique all: 4929 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
MOLREP9.2.10phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2CPP

2cpp


Resolution: 1.55→45.04 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.957 / SU B: 1.11 / SU ML: 0.041 / Isotropic thermal model: mixed / Cross valid method: THROUGHOUT / ESU R: 0.069 / ESU R Free: 0.07 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.18005 3818 5 %RANDOM
Rwork0.15506 ---
obs0.1563 71925 99.91 %-
all-75813 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 16.417 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 1.55→45.04 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3208 0 52 796 4056
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0223644
X-RAY DIFFRACTIONr_angle_refined_deg1.5012.0114964
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4685426
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.95124.255188
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.25315677
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.21531
X-RAY DIFFRACTIONr_chiral_restr0.0980.2528
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.022804
X-RAY DIFFRACTIONr_nbd_refined0.2330.22044
X-RAY DIFFRACTIONr_nbtor_refined0.3110.22516
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1190.2661
X-RAY DIFFRACTIONr_metal_ion_refined0.1790.24
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2040.243
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0810.245
X-RAY DIFFRACTIONr_mcbond_it0.6271.52122
X-RAY DIFFRACTIONr_mcangle_it1.08723512
X-RAY DIFFRACTIONr_scbond_it1.57331531
X-RAY DIFFRACTIONr_scangle_it2.4764.51452
LS refinement shellResolution: 1.551→1.591 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.222 272 -
Rwork0.183 5109 -
obs-4929 99.96 %

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