2r6k

Crystal structure of an I71V hGSTA1-1 mutant in complex with S-hexylglutathione

Method: X-RAY DIFFRACTION D_max: 65.5 Å Quality: EXCELLENT

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glutathione S-transferase A1

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–222 Chain B； UniProt 1–222	Mutation：I71V	GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；297 K；14 mg protein per ml, 0.1M Tris-HCl, 10 mM DTT, 19% PEG4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K	Resolution 2.51 Å R-free 0.298

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2R6K	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GSD GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM Deposited 1995-06-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.264
1GSD GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM Deposited 1995-06-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–221（221 aa） Chain D 1–221（221 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.264
1GSE GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K) Deposited 1995-06-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Mutation：R15K Mutation：R15K	GSH Glutathione × 2 EAA ETHACRYNIC ACID × 2 BME BETA-MERCAPTOETHANOL × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.243
1GSF GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID Deposited 1995-06-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Not recorded	EAA ETHACRYNIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.261
1GSF GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID Deposited 1995-06-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–221（221 aa） Chain D 1–221（221 aa）	Not recorded	EAA ETHACRYNIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.261
1GUH Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes Deposited 1993-02-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Not recorded	GSB S-BENZYL-GLUTATHIONE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1GUH Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes Deposited 1993-02-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–221（221 aa） Chain D 1–221（221 aa）	Not recorded	GSB S-BENZYL-GLUTATHIONE × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1K3L Crystal Structure Analysis of S-hexyl-glutathione Complex of Glutathione Transferase at 1.5 Angstroms Resolution Deposited 2001-10-03	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Not recorded	GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；294 K；18% PEG3350, 0.1 M Tris-Cl pH 7.5, 10mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 294K	Resolution 1.50 Å R-free 0.241
1K3O Crystal Structure Analysis of apo Glutathione S-Transferase Deposited 2001-10-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；22% PEG3350, 0.1M Tris-Cl 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 100K	Resolution 1.80 Å R-free 0.336
1K3Y Crystal Structure Analysis of human Glutathione S-transferase with S-hexyl glutatione and glycerol at 1.3 Angstrom Deposited 2001-10-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Not recorded	GTX S-HEXYLGLUTATHIONE × 2 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；15% PEG2000, 0.1M Tris-Cl 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 100K	Resolution 1.30 Å R-free 0.205
1LBK Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme Deposited 2002-04-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 208–213（6 aa） Chain B 208–213（6 aa）	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 GSH Glutathione × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；PEG 8000, calcium chloride, glutathione, (R,R)-1,4-dithiothreitol, 2-[N-morpholino]ethanesulphonic acid, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.86 Å R-free 0.224
1PKW Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione Deposited 2003-06-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GSH Glutathione × 2 HED 2-HYDROXYETHYL DISULFIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；PEG 4000, Tris HCl, 2-mercaptoethanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.208
1PKZ Crystal structure of human glutathione transferase (GST) A1-1 Deposited 2003-06-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	HED 2-HYDROXYETHYL DISULFIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；MethylPEG2000, Tris-HCl, NaAc, 2-mercaptoethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.10 Å R-free 0.230
1PL1 Crystal structure of human glutathione transferase (GST) A1-1 in complex with a decarboxy-glutathione Deposited 2003-06-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 2 ABY N-(4-AMINOBUTANOYL)-S-(4-METHOXYBENZYL)-L-CYSTEINYLGLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；PEG 4000, Tris-HCl, DTT, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.75 Å R-free 0.189
1PL2 Crystal structure of human glutathione transferase (GST) A1-1 T68E mutant in complex with decarboxy-glutathione Deposited 2003-06-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：T68E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：T68E Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 2 ABY N-(4-AMINOBUTANOYL)-S-(4-METHOXYBENZYL)-L-CYSTEINYLGLYCINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；PEG 4000, Tris-HCl, DTT, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.200
1USB Rational design of a novel enzyme - efficient thioester hydrolysis enabled by the incorporation of a single His residue into human glutathione transferase A1-1 Deposited 2003-11-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Mutation：YES Mutation：YES	GSH Glutathione × 2 CL CHLORIDE ION × 2 K POTASSIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；0.1 M TRISHCL PH 7.8, 26 % PEG4000, 2 MM DITHIOTHREITOL	Resolution 2.07 Å R-free 0.245
1XWG Human GST A1-1 T68E mutant Deposited 2004-11-01	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–222（221 aa） Chain B 2–222（221 aa）	Mutation：T68E Mutation：T68E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；293 K；PEG4 000, DTT, Tris-HCl, MPD, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.85 Å R-free 0.218
1YDK Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione Deposited 2004-12-24	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–221（221 aa） Chain B 1–221（221 aa）	Mutation：I219A Mutation：I219A	GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 2000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.95 Å R-free 0.253
2R3X Crystal structure of an R15L hGSTA1-1 mutant complexed with S-hexyl-glutathione Deposited 2007-08-30	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：R15L Mutation：R15L	GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；A 4uL hanging drop comprising: 2uL 14 mg/mL R15L hGSTA1-1 solution added to 2uL reservoir buffer (5mM S-hexyl-glutathione, 0.1M TrisHCl, pH 7.5, 10 mM DTT, 15% PEG 4000) was left to equilibrate in a sealed 24 plate well with 1 mL of reservoir buffer. Crystals were grown for 3 days before harvesting, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.80 Å R-free 0.259
3I69 Apo Glutathione Transferase A1-1 GIMF-helix mutant Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.38 Å R-free 0.289
3I69 Apo Glutathione Transferase A1-1 GIMF-helix mutant Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–222（222 aa） Chain D 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.38 Å R-free 0.289
3I69 Apo Glutathione Transferase A1-1 GIMF-helix mutant Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–222（222 aa） Chain F 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.38 Å R-free 0.289
3I69 Apo Glutathione Transferase A1-1 GIMF-helix mutant Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–222（222 aa） Chain H 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.38 Å R-free 0.289
3I6A Human GST A1-1 GIMF mutant with Glutathione Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, 10 mM DTT, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.244
3I6A Human GST A1-1 GIMF mutant with Glutathione Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–222（222 aa） Chain D 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, 10 mM DTT, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.244
3I6A Human GST A1-1 GIMF mutant with Glutathione Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–222（222 aa） Chain F 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, 10 mM DTT, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.244
3I6A Human GST A1-1 GIMF mutant with Glutathione Deposited 2009-07-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–222（222 aa） Chain H 1–222（222 aa）	Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P Mutation：A12G, L107I, L108M, V111F, M208P, K211I, S212Y, L213V, E214R, E215T, A216V, R217Y, K218N, F222P	GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 4000, 0.1 M Tric-Cl, 10 mM DTT, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.98 Å R-free 0.244
3IK9 Human GST A1-1-GIMF with GSDHN Deposited 2009-08-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Not recorded	BOB (S)-2-amino-5-((R)-1-(carboxymethylamino)-3-((3S,4R)-1,4-dihydroxynonan-3-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；16% PEG mme 5000, 0.1 M HEPES, pH 7.5, and 10% isopropanol, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.20 Å R-free 0.279
3IK9 Human GST A1-1-GIMF with GSDHN Deposited 2009-08-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–222（222 aa） Chain D 1–222（222 aa）	Not recorded	BOB (S)-2-amino-5-((R)-1-(carboxymethylamino)-3-((3S,4R)-1,4-dihydroxynonan-3-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；16% PEG mme 5000, 0.1 M HEPES, pH 7.5, and 10% isopropanol, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.20 Å R-free 0.279
3IK9 Human GST A1-1-GIMF with GSDHN Deposited 2009-08-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–222（222 aa） Chain F 1–222（222 aa）	Not recorded	BOB (S)-2-amino-5-((R)-1-(carboxymethylamino)-3-((3S,4R)-1,4-dihydroxynonan-3-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；16% PEG mme 5000, 0.1 M HEPES, pH 7.5, and 10% isopropanol, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.20 Å R-free 0.279
3IK9 Human GST A1-1-GIMF with GSDHN Deposited 2009-08-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–222（222 aa） Chain H 1–222（222 aa）	Not recorded	BOB (S)-2-amino-5-((R)-1-(carboxymethylamino)-3-((3S,4R)-1,4-dihydroxynonan-3-ylthio)-1-oxopropan-2-ylamino)-5-oxopentanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；16% PEG mme 5000, 0.1 M HEPES, pH 7.5, and 10% isopropanol, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.20 Å R-free 0.279
3KTL Crystal Structure of an I71A human GSTA1-1 mutant in complex with S-hexylglutathione Deposited 2009-11-25	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–222（221 aa） Chain B 2–222（221 aa）	Mutation：I71A Mutation：I71A	GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；20% PEG 4000, 0.1M Tris-Cl PH 7.5, 0.02% NaN3, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.75 Å R-free 0.281
3L0H Crystal Structure Analysis of W21A mutant of human GSTA1-1 in complex with S-hexylglutathione Deposited 2009-12-10	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：W21A Mutation：W21A	GTX S-HEXYLGLUTATHIONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.4M Sodium citrate in 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.13 Å R-free 0.233
3Q74 Crystal Structure Analysis of the L7A Mutant of the Apo Form of Human Alpha Class Glutathione Transferase Deposited 2011-01-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–222（221 aa） Chain B 2–222（221 aa）	Mutation：L7A Mutation：L7A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 7.5；293 K；0.1 M Tris, 20% PEG 3350, 2 mM DTT, 0.02% azide, pH 7.5, hanging drop, temperature 293K	Resolution 1.79 Å R-free 0.271
3U6V Crystal Structure Analysis of L23A mutant of human GST A1-1 Deposited 2011-10-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：L23A Mutation：L23A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Tris, 20% PEG 3350, 2 mM DTT, 0.02% azide, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.20 Å R-free 0.288
3ZFB Crystal structure of the I75A mutant of human class alpha glutathione transferase in the apo form Deposited 2012-12-11	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M TRIS, 17% PEG 4000, 2 MM DTT, 0.02% AZIDE, PH 7.5, VAPOUR DIFFUSION, HANGING DROP, TEMPERATURE 293K	Resolution 1.86 Å R-free 0.285
3ZFL Crystal structure of the V58A mutant of human class alpha glutathione transferase in the apo form Deposited 2012-12-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M TRIS, 19% PEG 3350, 2 MM DTT, 0.02% AZIDE, PH 7.5, VAPOUR DIFFUSION, HANGING DROP, TEMPERATURE 293K	Resolution 1.88 Å R-free 0.289
4HJ2 Crystal Structure Analysis of GSTA1-1 in complex with chlorambucil Deposited 2012-10-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 4–220（217 aa） Chain B 4–220（217 aa）	Not recorded	LZ6 L-gamma-glutamyl-S-(2-{[4-(3-carboxypropyl)phenyl](2-chloroethyl)amino}ethyl)-L-cysteinylglycine × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å R-free 0.258
5JCU Crystal Structure of hGSTA1-1 with Glutathione Adduct of Phenethyl Isothiocyanate and Cystein Adduct of Phenethyl Isothiocyanate Deposited 2016-04-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–222（221 aa） Chain B 2–222（221 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GVX L-gamma-glutamyl-S-[(2-phenylethyl)carbamothioyl]-L-cysteinylglycine × 2 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；293 K；PEG 3350 20% (w/v), Sodium acetate 0.2 M	Resolution 1.93 Å R-free 0.240
5JCU Crystal Structure of hGSTA1-1 with Glutathione Adduct of Phenethyl Isothiocyanate and Cystein Adduct of Phenethyl Isothiocyanate Deposited 2016-04-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 2–222（221 aa） Chain D 2–222（221 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	GVX L-gamma-glutamyl-S-[(2-phenylethyl)carbamothioyl]-L-cysteinylglycine × 2 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；293 K；PEG 3350 20% (w/v), Sodium acetate 0.2 M	Resolution 1.93 Å R-free 0.240
5LCZ Chimeric GST Deposited 2016-06-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–53（53 aa） Fragment：UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222 Chain A 66–85（20 aa） Fragment：UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222 Chain A 214–222（9 aa） Fragment：UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222 Chain B 1–53（53 aa） Fragment：UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222 Chain B 66–85（20 aa） Fragment：UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222 Chain B 214–222（9 aa） Fragment：UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222	Not recorded	GSH Glutathione × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；289 K；PEG 4000 20% (w/v), ammonium citrate 0.2 M, pH 6.4	Resolution 2.33 Å R-free 0.268
5LD0 Chimeric GST Deposited 2016-06-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–85（85 aa） Fragment：UNP residues 1-85,UNP residues 86-213,UNP residues 214-222 Chain A 214–222（9 aa） Fragment：UNP residues 1-85,UNP residues 86-213,UNP residues 214-222	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；Sodium formate 0.15 M, PEG 4000 15% (w/v)	Resolution 1.60 Å R-free 0.201
6ATO Crystal structure of hGSTA1-1 complexed with GSH and MPD in each subunit Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–222（221 aa）	Not recorded	GSH Glutathione × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；PEG 200 MME, 25% (w/v), 0.1 M Tris HCl, pH 8.5	Resolution 1.55 Å R-free 0.208
6ATO Crystal structure of hGSTA1-1 complexed with GSH and MPD in each subunit Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–222（221 aa）	Not recorded	GSH Glutathione × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；PEG 200 MME, 25% (w/v), 0.1 M Tris HCl, pH 8.5	Resolution 1.55 Å R-free 0.208
6ATP Crystal structure of apo-hGSTA1-1 exhibiting a new conformation of C-terminal helix Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–222（221 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；PEG 2000 MME, 20% (w/v), 0.05 M Tris HCl, pH 8.5	Resolution 1.70 Å R-free 0.201
6ATP Crystal structure of apo-hGSTA1-1 exhibiting a new conformation of C-terminal helix Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–222（221 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；PEG 2000 MME, 20% (w/v), 0.05 M Tris HCl, pH 8.5	Resolution 1.70 Å R-free 0.201
6ATQ Crystal structure of apo-hGSTA1-1 exhibiting a new conformation of C-terminal helix Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–222（221 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；PEG 2000 MME, 25% (w/v), 0.1 M MES, 6.5	Resolution 2.00 Å R-free 0.235
6ATQ Crystal structure of apo-hGSTA1-1 exhibiting a new conformation of C-terminal helix Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–222（221 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；PEG 2000 MME, 25% (w/v), 0.1 M MES, 6.5	Resolution 2.00 Å R-free 0.235
6ATR Crystal structure of hGSTA1-1 complexed with two GSH analogues in each subunit Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–222（221 aa）	Not recorded	BWS L-gamma-glutamyl-L-alanylglycine × 1 GSN 2-AMINO-5-[1-(CARBOXYLATOMETHYLCARBAMOYL)-2-NITROSOSULFANYL-ETHYL]AMINO-5-OXO-PENTANOATE × 1 EDO 1,2-ETHANEDIOL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；PEG 2000 MME, 25% (w/v), 0.1 M MES, pH 6.5	Resolution 1.29 Å R-free 0.182
6ATR Crystal structure of hGSTA1-1 complexed with two GSH analogues in each subunit Deposited 2017-08-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–222（221 aa）	Not recorded	BWS L-gamma-glutamyl-L-alanylglycine × 1 GSN 2-AMINO-5-[1-(CARBOXYLATOMETHYLCARBAMOYL)-2-NITROSOSULFANYL-ETHYL]AMINO-5-OXO-PENTANOATE × 1 EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；PEG 2000 MME, 25% (w/v), 0.1 M MES, pH 6.5	Resolution 1.29 Å R-free 0.182
6YAW Crystal structure of human GSTA1-1 bound to the glutathione adduct of cinnamaldehyde Deposited 2020-03-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Not recorded	P9H (2~{S})-2-azanyl-5-[[(2~{R})-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-3-[(1~{R})-3-oxidanylidene-1-phenyl-propyl]sulfanyl-propan-2-yl]amino]-5-oxidanylidene-pentanoic acid × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Tris-HCl 0.1M pH 7.5, PEG4000 18%	Resolution 2.19 Å R-free 0.247
7BIB Crystal structure of human GSTA1-1 bound to the glutathione adduct of hexyl-isothiocyanate Deposited 2021-01-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Not recorded	TZ8 (2~{R})-2-azanyl-5-[[(2~{R})-3-(hexylcarbamothioylsulfanyl)-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-propan-2-yl]amino]-5-oxidanylidene-pentanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Tris-HCl 0.1M pH 7.5, PEG4000 18%	Resolution 2.03 Å R-free 0.255
7BIC Crystal structure of human GSTA1-1 bound to allyl-isothiocyanate Deposited 2021-01-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Not recorded	9AI N-prop-2-en-1-ylthioformamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Tris-HCl 0.1M pH 7.5, PEG4000 18%	Resolution 2.46 Å R-free 0.277
7BIC Crystal structure of human GSTA1-1 bound to allyl-isothiocyanate Deposited 2021-01-12	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–222（222 aa） Chain D 1–222（222 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Tris-HCl 0.1M pH 7.5, PEG4000 18%	Resolution 2.46 Å R-free 0.277
8BHC K141H and S142H double mutant of hGSTA1-1 Deposited 2022-10-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–222（222 aa） Chain D 1–222（222 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；20% w/v PEG 3350, 0.2 lithium citrate tribasic tetrahydrate	Resolution 1.56 Å R-free 0.188
8BHC K141H and S142H double mutant of hGSTA1-1 Deposited 2022-10-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；20% w/v PEG 3350, 0.2 lithium citrate tribasic tetrahydrate	Resolution 1.56 Å R-free 0.188
8BHE K141H and S142H double mutant of hGSTA1-1 Deposited 2022-10-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–222（222 aa） Chain B 1–222（222 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；PEG 4000 17-20% w/v, Na malonate 0.2 M	Resolution 1.87 Å R-free 0.239

38 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GSTA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–222； UniProt 1–222 Author chain B； PDBConstruct 1–222； UniProt 1–222

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2r6k
Deposition date deposition_date	2007-09-06
Structure title title	Crystal structure of an I71V hGSTA1-1 mutant in complex with S-hexylglutathione
Keywords keywords	human Alpha class glutathione transferase 1-1, s-hexyl-glutathione, X-ray crystal structure, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	22.58 Å
Radius of gyration Rg (electron density) rg_electron	21.38 Å
Forward intensity I(0) i0	39132300.00
Molecular weight molecular_weight	51566.0 kDa
Excluded volume excluded_volume	65957 Å³
Envelope volume envelope_volume	75831 Å³
Hydration-shell volume shell_volume	28270 Å³
Envelope diameter envelope_diameter	67.1 Å
Shell Rg shell_rg	29.19 Å
Envelope Rg envelope_rg	21.42 Å
Shape Rg shape_rg	21.38 Å
Total Rg total_rg	22.32 Å
Total atoms total_atoms	3628
Residues n_residues	440
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	65.5 Å
Rg (real space) rg_real	22.40 Å
Rg uncertainty (real space) rg_real_error	0.21 Å
I(0) (real space) i0_real	3.9130e+07
I(0) uncertainty (real space) i0_real_error	4.4120e+05
Rg (reciprocal space) rg_reciprocal	22.45 Å
I(0) (reciprocal space) i0_reciprocal	39130000.0000
Solution quality estimate total_estimate	0.9087
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.8 Å
Skewness Skewness skewness	0.042
Kurtosis Kurtosis kurtosis	-0.550
Angular range angular_range	— – 0.3500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	10650000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.958

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Glutathione S-transferase A1
Molecular weight formula_weight	25656.1 kDa
EC 编号 ec_number	2.5.1.18
Mutation mutation	I71V
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3726

MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAVLNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	S-HEXYLGLUTATHIONE
Molecular weight formula_weight	392.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	98

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2r6ka1
Class class	a — All alpha proteins
Fold Fold fold	a.45 — GST C-terminal domain-like
Superfamily Superfamily superfamily	a.45.1 — GST C-terminal domain-like
Family Family family	a.45.1.1 — Glutathione S-transferase (GST), C-terminal domain

Domain ID domain_id	d2r6ka2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.47 — Thioredoxin fold
Superfamily Superfamily superfamily	c.47.1 — Thioredoxin-like
Family Family family	c.47.1.5 — Glutathione S-transferase (GST), N-terminal domain

Domain ID domain_id	d2r6kb1
Class class	a — All alpha proteins
Fold Fold fold	a.45 — GST C-terminal domain-like
Superfamily Superfamily superfamily	a.45.1 — GST C-terminal domain-like
Family Family family	a.45.1.1 — Glutathione S-transferase (GST), C-terminal domain

Domain ID domain_id	d2r6kb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.47 — Thioredoxin fold
Superfamily Superfamily superfamily	c.47.1 — Thioredoxin-like
Family Family family	c.47.1.5 — Glutathione S-transferase (GST), N-terminal domain

CATH v4.4 (4 domains)

Domain ID domain_id	2r6kA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	2r6kA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2r6kB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	2r6kB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Unit-cell length a length_a	98.409 Å
Unit-cell length b length_b	93.577 Å
Unit-cell length c length_c	50.717 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.05 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.510 Å
Low-resolution limit resolution_low	20.090 Å
R factor r_factor	0.2106
R_work r_work	0.2060
R_free r_free	0.2983

fit	/app/data/saxs_computation/r6/2r6k/2r6k.fit
pddf	/app/data/pr_computation/r6/2r6k/2r6k.pr.out
profile	/app/data/saxs_computation/r6/2r6k/2r6k.dat