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1gsy

GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE

Method: X-RAY DIFFRACTION Dmax: 65.4 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

GLUTATHIONE S-TRANSFERASE CLASS PI

OrganismNot specified

UniProt P19157

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 1–209 Chain B； UniProt 1–209 Not recorded GSH Glutathione × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.44 Å
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–209 Chain B； UniProt 1–209 Not recorded GSH Glutathione × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.44 Å

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 1GSY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BAY GLUTATHIONE S-TRANSFERASE YFYF CYS 47-CARBOXYMETHYLATED CLASS PI, FREE ENZYME Deposited 1996-11-02 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.236
1GLP 1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS Deposited 1994-03-07 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Not recorded GTS GLUTATHIONE SULFONIC ACID × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å
1GLQ 1.8 ANGSTROMS MOLECULAR STRUCTURE OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS Deposited 1994-03-07 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Not recorded GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
1GTI MODIFIED GLUTATHIONE S-TRANSFERASE (PI) COMPLEXED WITH S (P-NITROBENZYL)GLUTATHIONE Deposited 1998-01-09 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 1–209（209 aa）
Chain D 1–209（209 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.4；pH 6.4
Resolution 3.00 Å R-free 0.277
1GTI MODIFIED GLUTATHIONE S-TRANSFERASE (PI) COMPLEXED WITH S (P-NITROBENZYL)GLUTATHIONE Deposited 1998-01-09 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 1–209（209 aa）
Chain B 1–209（209 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.4；pH 6.4
Resolution 3.00 Å R-free 0.277
1GTI MODIFIED GLUTATHIONE S-TRANSFERASE (PI) COMPLEXED WITH S (P-NITROBENZYL)GLUTATHIONE Deposited 1998-01-09 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 1–209（209 aa）
Chain F 1–209（209 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.4；pH 6.4
Resolution 3.00 Å R-free 0.277
2GLR MOLECULAR STRUCTURE AT 1.8 ANGSTROMS OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS Deposited 1994-05-04 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Not recorded GTX S-HEXYLGLUTATHIONE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
2OA7 Mouse C14A Glutathione-S-Transferase Mutant in Complex with S-hexyl glutathione Deposited 2006-12-15 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Mutation：C14A Mutation：C14A GTX S-HEXYLGLUTATHIONE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.261
2OAC Mouse C14A Glutathione-S-Transferase Mutant in Complex with S-(p-nitrobenzyl) Glutathione Deposited 2006-12-15 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Mutation：C14A Mutation：C14A GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.259
2OAD Structure of Glutathione-S-Transferase C169A Mutant Deposited 2006-12-15 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–209（209 aa）
Chain B 1–209（209 aa）
Mutation：C169A Mutation：C169A GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å R-free 0.264
3O76 1.8 Angstroms molecular structure of mouse liver glutathione S-transferase mutant C47A complexed with S-(P-nitrobenzyl)glutathione Deposited 2010-07-30 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 2–210（209 aa）
Chain B 2–210（209 aa）
Mutation：C47A Mutation：C47A GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4；293 K；20% PEG 6000, 0.1 M sodium citrate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Resolution 1.77 Å R-free 0.223
8C5D Glutathione transferase P1-1 from Mus musculus Deposited 2023-01-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–210（210 aa）
Chain B 1–210（210 aa）
Not recorded GOL GLYCEROL × 2 GTB S-(P-NITROBENZYL)GLUTATHIONE × 2 NA SODIUM ION × 11 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；PEG 6000 20% (w/v), 0.2 M calcium chloride dihydrate, pH 8.0
Resolution 1.28 Å R-free 0.200

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GSTP1_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–209； UniProt 1–209 Author chain B； PDBConstruct 1–209； UniProt 1–209

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

SAXS profile for 1gsy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gsy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gsy
Deposition date deposition_date1996-10-25
Structure title titleGLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE
Keywords keywordsTRANSFERASE, MULTIGENE FAMILY; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.19 Å
Radius of gyration Rg (electron density) rg_electron21.17 Å
Forward intensity I(0) i036896100.00
Molecular weight molecular_weight47573.0 kDa
Excluded volume excluded_volume59826 ų
Envelope volume envelope_volume69661 ų
Hydration-shell volume shell_volume26471 ų
Envelope diameter envelope_diameter67.2 Å
Shell Rg shell_rg28.59 Å
Envelope Rg envelope_rg21.21 Å
Shape Rg shape_rg21.16 Å
Total Rg total_rg22.09 Å
Total atoms total_atoms3348
Residues n_residues418
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax65.4 Å
Rg (real space) rg_real22.00 Å
Rg uncertainty (real space) rg_real_error0.29 Å
I(0) (real space) i0_real3.6900e+07
I(0) uncertainty (real space) i0_real_error4.1180e+05
Rg (reciprocal space) rg_reciprocal22.03 Å
I(0) (reciprocal space) i0_reciprocal36900000.0000
Solution quality estimate total_estimate0.9102
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3 Å
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.3600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9630000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.995
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1gsya1
Class classa — All alpha proteins
Fold Fold folda.45 — GST C-terminal domain-like
Superfamily Superfamily superfamilya.45.1 — GST C-terminal domain-like
Family Family familya.45.1.1 — Glutathione S-transferase (GST), C-terminal domain
Domain ID domain_idd1gsya2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.5 — Glutathione S-transferase (GST), N-terminal domain
Domain ID domain_idd1gsyb1
Class classa — All alpha proteins
Fold Fold folda.45 — GST C-terminal domain-like
Superfamily Superfamily superfamilya.45.1 — GST C-terminal domain-like
Family Family familya.45.1.1 — Glutathione S-transferase (GST), C-terminal domain
Domain ID domain_idd1gsyb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.5 — Glutathione S-transferase (GST), N-terminal domain

CATH v4.4 (4 domains)

Domain ID domain_id1gsyA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1gsyA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily10 —
Domain ID domain_id1gsyB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1gsyB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily10 —
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8. Citations (1)

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9. Files and Curves (10)