Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T53510 Target Info
Target Name Glutathione S-transferase A2 (GSTA2)
Synonyms GTH2; GSTA2-2; GST2; GST-gamma; GST class-alpha member 2; GST HA subunit 2
Target Type Literature-reported Target
Gene Name GSTA2
UniProt ID
GSTA2_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Glutathione Ligand Info
Structure Description Crystal structure of mutant GST A2-2 with enhanced catalytic efficiency with azathioprine PDB:4ACS
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [1]
PDB Sequence
KPKLHYSNIR
13
GRMESIRWLL
23
AAAGVEFEEK
33
FIKSAEDLDK
43
LRNDGYLMFQ
53

QVPMVEIDGM
63
KLVQTRAILN
73
YIASKYNLYG
83
KDIKEKALID
93
MYIEGIADLG
103

EMIGDLSFSQ
113
PEEQDAKLAL
123
IQEKTKNRYF
133
PAFEKVLKSH
143
GQDYLVGNKL
153

SRADIHLVEL
163
LYYVEELDSS
173
LISSFPLLKA
183
LKTRISNLPT
193
VKKFLQPGSP
203

RKPPMDEKSL
213
EESRKIFRH
Residue
Distance (Å)
TYR9
3.223
ARG15
3.874
LEU41
4.348
ARG45
2.995
GLN53
3.920
GLN54
3.187
Residue
Distance (Å)
VAL55
2.592
PRO56
3.536
GLN67
2.672
THR68
2.461
ARG69
4.940
PHE220
3.234
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 4-ANDROSTENE-3-17-DIONE Ligand Info
Structure Description Glutathione transferase A2-2 in complex with delta-4-andostrene-3-17- dione PDB:2VCT
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [2]
PDB Sequence
AEKPKLHYSN
11
IRGRMESIRW
21
LLAAAGVEFE
31
EKFIKSAEDL
41
DKLRNDGYLM
51

FQQVPMVEID
61
GMKLVQTRAI
71
LNYIASKYNL
81
YGKDIKEKAL
91
IDMYIEGIAD
101

LGEMILLLPF
111
TQPEEQDAKL
121
ALIQEKTKNR
131
YFPAFEKVLK
141
SHGQDYLVGN
151

KLSRADIHLV
161
ELLYYVEELD
171
SSLISSFPLL
181
KALKTRISNL
191
PTVKKFLQPG
201

SPRKPPMDEK
211
SLEESRKIFR
221
F
Residue
Distance (Å)
TYR9
3.356
ILE12
3.846
GLY14
3.079
ARG15
3.596
LEU107
3.659
LEU108
3.537
Residue
Distance (Å)
PHE111
3.265
THR112
4.756
SER216
4.948
PHE220
3.865
PHE222
3.184
Ligand Name: S-hexylglutathione Ligand Info
Structure Description A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL PDB:1AGS
Method X-ray diffraction Resolution 2.50 Å Mutation No [3]
PDB Sequence
AEKPKLHYFN
10
ARGRMESTRW
20
LLAAAGVEFE
30
EKFIKSAEDL
40
DKLRNDGYLM
50

FQQVPMVEID
60
GMKLVQTRAI
70
LNYIASKYNL
80
YRKDIKEKAL
90
IDMYIEGIAD
100

LGEMILLLPF
110
TQPEEQDAKL
120
ALIKEKIKNR
130
YFPAFEKVLK
140
SHGQDYLVGN
150

KLSRADIHLV
160
ELLYYVEELD
170
SSLISSFPLL
180
KALKTRISNL
190
PTVKKFLQPG
200

SPRKPPMDEK
210
SLEEARKIFR
220
F
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GTX or .GTX2 or .GTX3 or :3GTX;style chemicals stick;color identity;select .A:53 or .A:54 or .A:66 or .A:67; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLN53
2.963
VAL54
4.265
Residue
Distance (Å)
GLN66
3.186
THR67
4.223
References  Top
REF 1 Structure-based redesign of GST A2-2 for enhanced catalytic efficiency with azathioprine. Chem Biol. 2012 Mar 23;19(3):414-21.
REF 2 Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases. J Mol Biol. 2010 Mar 19;397(1):332-40.
REF 3 A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins. 1994 Nov;20(3):259-63.

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