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- PDB-3pcv: Crystal structure analysis of human leukotriene C4 synthase at 1.... -

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Basic information

Entry
Database: PDB / ID: 3pcv
TitleCrystal structure analysis of human leukotriene C4 synthase at 1.9 angstrom resolution
ComponentsLeukotriene C4 synthase
KeywordsLYASE / membrane protein / helix bundle / homo trimer / mGST / MAPEG
Function / homology
Function and homology information


Biosynthesis of protectin and resolvin conjugates in tissue regeneration (PCTR and RCTR) / Biosynthesis of maresin conjugates in tissue regeneration (MCTR) / leukotriene-C4 synthase / leukotriene-C4 synthase activity / Synthesis of 5-eicosatetraenoic acids / Biosynthesis of Lipoxins (LX) / leukotriene metabolic process / Transferases; Transferring alkyl or aryl groups, other than methyl groups / Synthesis of Leukotrienes (LT) and Eoxins (EX) / glutathione peroxidase activity ...Biosynthesis of protectin and resolvin conjugates in tissue regeneration (PCTR and RCTR) / Biosynthesis of maresin conjugates in tissue regeneration (MCTR) / leukotriene-C4 synthase / leukotriene-C4 synthase activity / Synthesis of 5-eicosatetraenoic acids / Biosynthesis of Lipoxins (LX) / leukotriene metabolic process / Transferases; Transferring alkyl or aryl groups, other than methyl groups / Synthesis of Leukotrienes (LT) and Eoxins (EX) / glutathione peroxidase activity / leukotriene biosynthetic process / long-chain fatty acid biosynthetic process / nuclear outer membrane / glutathione transferase activity / enzyme activator activity / nuclear envelope / nuclear membrane / intracellular membrane-bounded organelle / lipid binding / endoplasmic reticulum membrane / endoplasmic reticulum / identical protein binding / membrane
Similarity search - Function
5-lipoxygenase-activating protein / FLAP/GST2/LTC4S, conserved site / FLAP/GST2/LTC4S family signature. / : / Membrane associated eicosanoid/glutathione metabolism-like domain / Membrane-associated, eicosanoid/glutathione metabolism (MAPEG) protein / Membrane associated eicosanoid/glutathione metabolism-like domain superfamily / MAPEG family / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
GLUTATHIONE / Unknown ligand / Leukotriene C4 synthase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsSaino, H. / Ago, H. / Miyano, M.
Citation
Journal: J.Biol.Chem. / Year: 2011
Title: The catalytic architecture of leukotriene C4 synthase with two arginine residues
Authors: Saino, H. / Ukita, Y. / Ago, H. / Irikura, D. / Nisawa, A. / Ueno, G. / Yamamoto, M. / Kanaoka, Y. / Lam, B.K. / Austen, K.F. / Miyano, M.
#1: Journal: Nature / Year: 2007
Title: Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis
Authors: Ago, H. / Kanaoka, Y. / Irikura, D. / Lam, B.K. / Shimamura, T. / Austen, K.F. / Miyano, M.
History
DepositionOct 22, 2010Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 16, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 14, 2011Group: Database references / Non-polymer description
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_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _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

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Assembly

Deposited unit
A: Leukotriene C4 synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,77623
Polymers17,4121
Non-polymers6,36422
Water1,69394
1
A: Leukotriene C4 synthase
hetero molecules

A: Leukotriene C4 synthase
hetero molecules

A: Leukotriene C4 synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,32869
Polymers52,2353
Non-polymers19,09366
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation18_555z,-x+1/2,-y+1/21
crystal symmetry operation48_555-y+1/2,-z+1/2,x1
Buried area5870 Å2
ΔGint-60 kcal/mol
Surface area20670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)168.0295, 168.0295, 168.0295
Angle α, β, γ (deg.)90.0, 90.0, 90.0
Int Tables number196
Space group name H-MF23
Components on special symmetry positions
IDModelComponents
11A-251-

SO4

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Components

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Protein / Sugars , 2 types, 12 molecules A

#1: Protein Leukotriene C4 synthase / LTC4 synthase / Leukotriene-C(4) synthase


Mass: 17411.539 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LTC4S / Plasmid: pESP / Production host: Schizosaccharomyces pombe (fission yeast) / References: UniProt: Q16873, leukotriene-C4 synthase
#3: Sugar
ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM

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Non-polymers , 5 types, 105 molecules

#2: Chemical ChemComp-GSH / GLUTATHIONE


Mass: 307.323 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N3O6S
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical
ChemComp-UNL / UNKNOWN LIGAND


Num. of mol.: 4 / Source method: obtained synthetically
#6: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 94 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsLIGANDS ASSINGED UNL IN THE COORDINATES WERE SUPPOSED TO BE THE MALTOSIDE PORTIONS OF DODECYL ...LIGANDS ASSINGED UNL IN THE COORDINATES WERE SUPPOSED TO BE THE MALTOSIDE PORTIONS OF DODECYL MALTOSIDE, BUT THE ELECTRON DENSITY WAS NOT ENOUGH TO DETERMINE THE CORRECT ORIENTATIONS OF THE MALTOSIDE GROUPS.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 4.91 Å3/Da / Density % sol: 74.77 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1M MES-NaOH (pH 6.5), 1.6M ammonium sulfate, 0.8M magnesium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B2 / Wavelength: 0.97 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 5, 2008
RadiationMonochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 1.9→20.4 Å / Num. obs: 30950 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.9 % / Rmerge(I) obs: 0.08
Reflection shellResolution: 1.9→2 Å / Redundancy: 7.7 % / Rmerge(I) obs: 0.302 / Num. unique all: 4517 / % possible all: 100

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Processing

Software
NameVersionClassification
BSSdata collection
AMoREphasing
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2UUI

2uui


Resolution: 1.9→18.78 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.947 / SU B: 1.6 / SU ML: 0.049 / Cross valid method: THROUGHOUT / ESU R Free: 0.084 / Stereochemistry target values: MON_LIB in CCP4
RfactorNum. reflection% reflectionSelection details
Rfree0.19763 1568 5.1 %RANDOM
Rwork0.17819 ---
all0.17919 30949 --
obs0.17919 29381 99.97 %-
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: 29.263 Å2
Refinement stepCycle: LAST / Resolution: 1.9→18.78 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1110 0 156 94 1360
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_refined_d0.013
X-RAY DIFFRACTIONr_angle_refined_deg1.174
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.119
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.661
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.317
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.514
X-RAY DIFFRACTIONr_chiral_restr0.086
X-RAY DIFFRACTIONr_gen_planes_refined0.008
X-RAY DIFFRACTIONr_mcbond_it2.651
X-RAY DIFFRACTIONr_mcangle_it3.361
X-RAY DIFFRACTIONr_scbond_it4.62
X-RAY DIFFRACTIONr_scangle_it6.338
LS refinement shellResolution: 1.901→1.949 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.246 113 -
Rwork0.225 2161 -
obs--100 %

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