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- PDB-16gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3 -

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Basic information

Entry
Database: PDB / ID: 16gs
TitleGLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
ComponentsGLUTATHIONE S-TRANSFERASE
KeywordsTRANSFERASE / APOENZYME / DETOXIFICATION
Function / homology
Function and homology information


nitric oxide storage / negative regulation of smooth muscle cell chemotaxis / S-nitrosoglutathione binding / negative regulation of leukocyte proliferation / negative regulation of biosynthetic process / kinase regulator activity / dinitrosyl-iron complex binding / TRAF2-GSTP1 complex / cellular response to cell-matrix adhesion / common myeloid progenitor cell proliferation ...nitric oxide storage / negative regulation of smooth muscle cell chemotaxis / S-nitrosoglutathione binding / negative regulation of leukocyte proliferation / negative regulation of biosynthetic process / kinase regulator activity / dinitrosyl-iron complex binding / TRAF2-GSTP1 complex / cellular response to cell-matrix adhesion / common myeloid progenitor cell proliferation / negative regulation of monocyte chemotactic protein-1 production / hepoxilin biosynthetic process / linoleic acid metabolic process / glutathione derivative biosynthetic process / response to L-ascorbic acid / negative regulation of nitric-oxide synthase biosynthetic process / negative regulation of JUN kinase activity / nitric oxide binding / Glutathione conjugation / oligodendrocyte development / JUN kinase binding / glutathione peroxidase activity / negative regulation of MAPK cascade / negative regulation of stress-activated MAPK cascade / negative regulation of interleukin-1 beta production / cellular response to glucocorticoid stimulus / prostaglandin metabolic process / regulation of stress-activated MAPK cascade / negative regulation of tumor necrosis factor-mediated signaling pathway / Detoxification of Reactive Oxygen Species / glutathione transferase / negative regulation of tumor necrosis factor production / glutathione transferase activity / negative regulation of acute inflammatory response / negative regulation of vascular associated smooth muscle cell proliferation / negative regulation of fibroblast proliferation / xenobiotic metabolic process / fatty acid binding / animal organ regeneration / response to amino acid / central nervous system development / negative regulation of I-kappaB kinase/NF-kappaB signaling / regulation of ERK1 and ERK2 cascade / cellular response to epidermal growth factor stimulus / negative regulation of ERK1 and ERK2 cascade / glutathione metabolic process / positive regulation of superoxide anion generation / negative regulation of MAP kinase activity / response to reactive oxygen species / negative regulation of extrinsic apoptotic signaling pathway / negative regulation of protein kinase activity / cellular response to insulin stimulus / response to estradiol / secretory granule lumen / response to ethanol / vesicle / ficolin-1-rich granule lumen / cellular response to lipopolysaccharide / Neutrophil degranulation / negative regulation of apoptotic process / mitochondrion / extracellular space / extracellular exosome / extracellular region / plasma membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
Glutathione S-transferase, Pi class / Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione Transferase family / Glutathione S-transferase, C-terminal / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 - #10 / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 ...Glutathione S-transferase, Pi class / Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione Transferase family / Glutathione S-transferase, C-terminal / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 - #10 / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / Up-down Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Glutathione S-transferase P
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsOakley, A.J. / Lo Bello, M. / Ricci, G. / Federici, G. / Parker, M.W.
CitationJournal: Biochemistry / Year: 1998
Title: Evidence for an induced-fit mechanism operating in pi class glutathione transferases.
Authors: Oakley, A.J. / Lo Bello, M. / Ricci, G. / Federici, G. / Parker, M.W.
History
DepositionNov 30, 1997-
Revision 1.0Jan 13, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GLUTATHIONE S-TRANSFERASE
B: GLUTATHIONE S-TRANSFERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,2425
Polymers46,7562
Non-polymers4873
Water5,368298
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2850 Å2
ΔGint-33 kcal/mol
Surface area17960 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)77.537, 89.797, 68.673
Angle α, β, γ (deg.)90.00, 97.79, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.939833, 0.129827, 0.316003), (0.128491, -0.991391, 0.025155), (0.316549, 0.016962, -0.948424)
Vector: -5.89306, 21.18149, 27.19538)

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Components

#1: Protein GLUTATHIONE S-TRANSFERASE / / GSTP1-1


Mass: 23377.770 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOSOL / Gene: GSTP1 / Gene (production host): GSTP1 / Production host: Escherichia coli (E. coli) / References: UniProt: P09211, glutathione transferase
#2: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 298 / 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: 2.53 Å3/Da / Density % sol: 51.42 %
Crystal growpH: 5.8 / Details: pH 5.8
Crystal grow
*PLUS
Temperature: 22 ℃ / pH: 7 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
112 mg/mlprotein1drop
210 mMphosphate1drop
31 mMEDTA1drop
42 mMbeta-mercaptoethanol1drop
523 %(w/v)ammonium sulfate1reservoir
655 mMdithiothreitol1reservoir
7100 mMMES1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 25, 1997
RadiationMonochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.9→14 Å / Num. obs: 96823 / % possible obs: 95.1 % / Observed criterion σ(I): -3 / Redundancy: 2.8 % / Biso Wilson estimate: 21 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 17.7
Reflection shellResolution: 1.91→1.98 Å / Rmerge(I) obs: 0.329 / Mean I/σ(I) obs: 2.6 / % possible all: 91.5
Reflection
*PLUS
Num. obs: 31323 / Num. measured all: 96823
Reflection shell
*PLUS
% possible obs: 91.5 %

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Processing

Software
NameVersionClassification
X-PLOR3.851model building
X-PLOR3.851refinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLOR3.851phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 5GSS
Resolution: 1.9→15 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 100000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflectionSelection details
Rfree0.263 1705 5 %RANDOM
Rwork0.227 ---
obs0.227 34299 93.5 %-
Displacement parametersBiso mean: 27.2 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.29 Å0.25 Å
Luzzati d res low-15 Å
Luzzati sigma a0.28 Å0.28 Å
Refinement stepCycle: LAST / Resolution: 1.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3262 0 29 1631 4922
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONx_bond_d0.007
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.3
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d23.2
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d0.82
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it2.141.5
X-RAY DIFFRACTIONx_mcangle_it3.12
X-RAY DIFFRACTIONx_scbond_it3.752
X-RAY DIFFRACTIONx_scangle_it5.342.5
Refine LS restraints NCSNCS model details: RESTRAINTS
LS refinement shellResolution: 1.9→1.97 Å / Rfactor Rfree error: 0.031 / Total num. of bins used: 10
RfactorNum. reflection% reflection
Rfree0.36 139 5 %
Rwork0.366 2641 -
obs--75.8 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMTOPHCSDX.PRO
X-RAY DIFFRACTION2WATER.MES.TO
X-RAY DIFFRACTION3MES.PAWATER.
X-RAY DIFFRACTION4SO4.PASO4.TO
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refinement
*PLUS
Num. reflection obs: 32594
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_angle_deg1.28
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg23.2
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg0.82

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