CATH Classification
Level | CATH Code | Description |
---|---|---|
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1 | Mainly Alpha |
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1.20 | Up-down Bundle |
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1.20.1050 | Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 |
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1.20.1050.10 |
Domain Context
CATH Clusters
Superfamily | 1.20.1050.10 |
Functional Family | Glutathione S-transferase A1 |
Enzyme Information
2.5.1.18 |
Glutathione transferase.
based on mapping to UniProt P08263
RX + glutathione = HX + R-S-glutathione.
-!- A group of enzymes of broad specificity. -!- R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. -!- Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. -!- Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7.
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1.11.1.- |
Peroxidases.
based on mapping to UniProt P08263
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5.3.3.- |
Transposing C=C bonds.
based on mapping to UniProt P08263
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UniProtKB Entries (1)
P08263 |
GSTA1_HUMAN
Homo sapiens
Glutathione S-transferase A1
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PDB Structure
PDB | 1YDK |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Tertiary Interactions Stabilise the C-terminal Region of Human Glutathione Transferase A1-1: a Crystallographic and Calorimetric Study.
J.Mol.Biol.
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