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- PDB-1gsc: NEW CRYSTAL FORMS OF A MU CLASS GLUTATHIONE S-TRANSFERASE FROM RA... -

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Basic information

Entry
Database: PDB / ID: 1gsc
TitleNEW CRYSTAL FORMS OF A MU CLASS GLUTATHIONE S-TRANSFERASE FROM RAT LIVER
ComponentsGLUTATHIONE S-TRANSFERASE
KeywordsTRANSFERASE(GLUTATHIONE)
Function / homology
Function and homology information


Glutathione conjugation / nitrobenzene metabolic process / cellular detoxification of nitrogen compound / hepoxilin biosynthetic process / glutathione derivative biosynthetic process / glutathione binding / response to metal ion / prostaglandin metabolic process / glutathione transferase / nickel cation binding ...Glutathione conjugation / nitrobenzene metabolic process / cellular detoxification of nitrogen compound / hepoxilin biosynthetic process / glutathione derivative biosynthetic process / glutathione binding / response to metal ion / prostaglandin metabolic process / glutathione transferase / nickel cation binding / glutathione transferase activity / response to amino acid / response to axon injury / xenobiotic catabolic process / steroid binding / glutathione metabolic process / response to lead ion / sensory perception of smell / cellular response to xenobiotic stimulus / response to ethanol / response to xenobiotic stimulus / protein kinase binding / enzyme binding / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular region / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Glutathione S-transferase, Mu class / Glutathione S-transferase, C-terminal domain / : / Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal ...Glutathione S-transferase, Mu class / Glutathione S-transferase, C-terminal domain / : / Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Thioredoxin-like superfamily
Similarity search - Domain/homology
Glutathione S-transferase Mu 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / Resolution: 2.5 Å
AuthorsFu, J.-H. / Rose, J.P. / Wang, B.-C.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 1994
Title: New crystal forms of a mu-class glutathione S-transferase from rat liver.
Authors: Fu, J.H. / Rose, J. / Tam, M.F. / Wang, B.C.
#1: Journal: Acta Crystallogr.,Sect.B / Year: 1991
Title: Crystals of Isoenzyme 3-3 of Rat Liver Glutathione S-Transferase with and without Inhibitor
Authors: Fu, J.-H. / Rose, J. / Chung, Y.-J. / Tam, M.F. / Wang, B.-C.
History
DepositionSep 8, 1993Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GLUTATHIONE S-TRANSFERASE
B: GLUTATHIONE S-TRANSFERASE
C: GLUTATHIONE S-TRANSFERASE
D: GLUTATHIONE S-TRANSFERASE


Theoretical massNumber of molelcules
Total (without water)103,2754
Polymers103,2754
Non-polymers00
Water00
1
A: GLUTATHIONE S-TRANSFERASE
B: GLUTATHIONE S-TRANSFERASE


Theoretical massNumber of molelcules
Total (without water)51,6382
Polymers51,6382
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: GLUTATHIONE S-TRANSFERASE
D: GLUTATHIONE S-TRANSFERASE


Theoretical massNumber of molelcules
Total (without water)51,6382
Polymers51,6382
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)97.377, 81.109, 69.425
Angle α, β, γ (deg.)90.00, 109.16, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
GLUTATHIONE S-TRANSFERASE / Coordinate model: Cα atoms only


Mass: 25818.791 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: LIVER / References: UniProt: P04905, glutathione transferase

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 50.93 %
Crystal grow
*PLUS
Temperature: 291 K / pH: 8 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
120 %(w/v)PEG33501reservoir
2100 mMHEPES1reservoir
310 mMbeta-octylglucopyranoside1drop
40.6 mMethylmercury chloride1drop

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Processing

RefinementHighest resolution: 2.5 Å
Refinement stepCycle: LAST / Highest resolution: 2.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms868 0 0 0 868

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