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- PDB-5jkw: HUMAN PLACENTAL AROMATASE CYTOCHROME P450 (CYP19A1) COMPLEXED WIT... -

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Basic information

Entry
Database: PDB / ID: 5jkw
TitleHUMAN PLACENTAL AROMATASE CYTOCHROME P450 (CYP19A1) COMPLEXED WITH TESTOSTERONE
ComponentsAromatase
KeywordsOXIDOREDUCTASE / Aromatase / cytochrome P450 / human placenta / estrogen synthase / testosterone
Function / homology
Function and homology information


aromatase / Defective CYP19A1 causes AEXS / positive regulation of estradiol secretion / androgen catabolic process / female genitalia development / syncytium formation / estrogen biosynthetic process / negative regulation of chronic inflammatory response / Estrogen biosynthesis / testosterone biosynthetic process ...aromatase / Defective CYP19A1 causes AEXS / positive regulation of estradiol secretion / androgen catabolic process / female genitalia development / syncytium formation / estrogen biosynthetic process / negative regulation of chronic inflammatory response / Estrogen biosynthesis / testosterone biosynthetic process / sterol metabolic process / prostate gland growth / negative regulation of macrophage chemotaxis / mammary gland development / steroid biosynthetic process / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen / steroid hydroxylase activity / aromatase activity / female gonad development / uterus development / Endogenous sterols / oxygen binding / response to estradiol / electron transfer activity / iron ion binding / heme binding / endoplasmic reticulum membrane / endoplasmic reticulum / membrane
Similarity search - Function
Cytochrome P450, E-class, group I / 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
PROTOPORPHYRIN IX CONTAINING FE / TESTOSTERONE / Aromatase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 3 Å
AuthorsGhosh, D. / Egbuta, C. / Lo, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM086893 United States
CitationJournal: J. Steroid Biochem. Mol. Biol. / Year: 2018
Title: Testosterone complex and non-steroidal ligands of human aromatase.
Authors: Ghosh, D. / Egbuta, C. / Lo, J.
History
DepositionApr 26, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 26, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2May 30, 2018Group: Data collection / Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.3Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Aromatase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,8603
Polymers57,9551
Non-polymers9052
Water1267
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)140.523, 140.523, 118.471
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein Aromatase / / CYPXIX / Cytochrome P-450AROM / Cytochrome P450 19A1 / Estrogen synthase


Mass: 57954.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P11511, aromatase
#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-TES / TESTOSTERONE / Testosterone


Mass: 288.424 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H28O2 / Comment: hormone*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 7 / 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: 5.83 Å3/Da / Density % sol: 78.89 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.4 / Details: 20-30% PEG 4000, PHOSPHATE BUFFER, PH 7.4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 20, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 3→30.5 Å / Num. obs: 24964 / % possible obs: 95.7 % / Redundancy: 3.6 % / Net I/σ(I): 23.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0131refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 3S79
Resolution: 3→30.5 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.932 / SU B: 11.638 / SU ML: 0.201 / Cross valid method: THROUGHOUT / ESU R: 0.373 / ESU R Free: 0.266 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22234 1271 4.8 %RANDOM
Rwork0.19686 ---
obs0.19814 24964 95.57 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 88.892 Å2
Baniso -1Baniso -2Baniso -3
1-1.65 Å20.82 Å20 Å2
2--1.65 Å20 Å2
3----5.34 Å2
Refinement stepCycle: 1 / Resolution: 3→30.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3658 0 64 7 3729
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0193824
X-RAY DIFFRACTIONr_bond_other_d0.0020.023748
X-RAY DIFFRACTIONr_angle_refined_deg1.4071.9935174
X-RAY DIFFRACTIONr_angle_other_deg0.96838630
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.9595453
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.9723.554166
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.61315712
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.2691525
X-RAY DIFFRACTIONr_chiral_restr0.0870.2568
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0214203
X-RAY DIFFRACTIONr_gen_planes_other0.0040.02880
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_it3.7658.6581812
X-RAY DIFFRACTIONr_mcbond_other3.7638.6551811
X-RAY DIFFRACTIONr_mcangle_it5.91512.992265
X-RAY DIFFRACTIONr_mcangle_other5.91512.9932266
X-RAY DIFFRACTIONr_scbond_it4.169.1032012
X-RAY DIFFRACTIONr_scbond_other4.1599.1022013
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.81713.4422910
X-RAY DIFFRACTIONr_long_range_B_refined9.32168.5024347
X-RAY DIFFRACTIONr_long_range_B_other9.31568.5014345
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3→3.077 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.376 88 -
Rwork0.33 1881 -
obs--99.19 %

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