DB code: D00531

CATH domain 3.40.30.10 : Glutaredoxin Catalytic domain
1.20.1050.10 : Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
E.C. 2.5.1.18
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
Q8MU52 Glutathione S-transferase
EC 2.5.1.18
PfGST
PF00043 (GST_C)
PF02798 (GST_N)
[Graphical View]

KEGG enzyme name
S-(Hydroxylalkyl)-glutathione liase
Glutathione S-aralkyltransferase
Glutathione S-alkyl transferase
Glutathione transferase
Glutathione S-transferase
Glutathione S-alkyltransferase
Glutathione S-aryltransferase
GST

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q8MU52 GST_PLAFA RX + GLUTATHIONE = HX + R-S-GLUTATHIONE. Homodimer. In the absence of ligands two homodimers may interact to form a tetramer.

KEGG Pathways
Map code Pathways E.C.
MAP00480 Glutathione metabolism
MAP00980 Metabolism of xenobiotics by cytochrome P450
MAP00982 Drug metabolism - cytochrome P450

Compound table
Substrates Products Intermediates
KEGG-id C01322 C00051 C01318 C02320
E.C.
Compound RX Glutathione HX R-S-Glutathione
Type halide amino acids,carboxyl group,peptide/protein,sulfhydryl group halide amide group,carboxyl group,peptide/protein,sulfide group
ChEBI 16856
PubChem 124886
25246407
1oktA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1oktB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pa3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pa3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1q4jA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:GTX
1q4jB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:GTX
2aawA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:GTX
2aawC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:GTX
3fr3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:GDS
3fr3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:GDS
3fr6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr6B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:GSH Unbound Unbound Unbound
3fr9B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:GSH Unbound Unbound Unbound
3frcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:0HG
3frcB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:0HG
1oktA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1oktB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pa3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1pa3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1q4jA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1q4jB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2aawA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2aawC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr6B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3fr9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:_CL Unbound
3fr9B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:_CL Unbound
3frcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3frcB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [8], [9], [11] & [13]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1oktA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
1oktB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
1pa3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
1pa3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
1q4jA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
1q4jB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
2aawA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
2aawC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3fr3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3fr3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3fr6A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3fr6B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3fr9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3fr9B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3frcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
3frcB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 9
1oktA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1oktB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pa3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1pa3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1q4jA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1q4jB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2aawA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2aawC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3fr3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3fr3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3fr6A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3fr6B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3fr9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3fr9B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3frcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3frcB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
[3]
p.652-3
[4]
[8]
p.13823-5, Fig.3, Fig.4
[12]

References
[1]
Resource
Comments Review
Medline ID
PubMed ID 1782341
Journal Chem Res Toxicol
Year 1991
Volume 4
Pages 131-40
Authors Armstrong RN
Title Glutathione S-transferases: reaction mechanism, structure, and function.
Related PDB
Related UniProtKB
[2]
Resource
Comments Review
Medline ID
PubMed ID 1771176
Journal Pharmacol Ther
Year 1991
Volume 51
Pages 35-46
Authors van Bladeren PJ, van Ommen B
Title The inhibition of glutathione S-transferases: mechanisms, toxic consequences and therapeutic benefits.
Related PDB
Related UniProtKB
[3]
Resource
Comments Review
Medline ID
PubMed ID 8143720
Journal Eur J Biochem
Year 1994
Volume 220
Pages 645-61
Authors Dirr H, Reinemer P, Huber R
Title X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
Related PDB
Related UniProtKB
[4]
Resource
Comments Review
Medline ID
PubMed ID 9074797
Journal Chem Res Toxicol
Year 1997
Volume 10
Pages 2-18
Authors Armstrong RN
Title Structure, catalytic mechanism, and evolution of the glutathione transferases.
Related PDB
Related UniProtKB
[5]
Resource
Comments Review
Medline ID
PubMed ID 16399376
Journal Methods Enzymol
Year 2005
Volume 401
Pages 1-8
Authors Mannervik B, Board PG, Hayes JD, Listowsky I, Pearson WR
Title Nomenclature for mammalian soluble glutathione transferases.
Related PDB
Related UniProtKB
[6]
Resource
Comments Review
Medline ID
PubMed ID 17897613
Journal Acta Trop
Year 2008
Volume 105
Pages 99-112
Authors Torres-Rivera A, Landa A
Title Glutathione transferases from parasites: a biochemical view.
Related PDB
Related UniProtKB
[7]
Resource
Comments Review
Medline ID
PubMed ID 18691123
Journal Curr Protein Pept Sci
Year 2008
Volume 9
Pages 325-37
Authors Dourado DF, Fernandes PA, Ramos MJ
Title Mammalian cytosolic glutathione transferases.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND CATALYTIC ACTIVITY.
Medline ID
PubMed ID 14623980
Journal Proc Natl Acad Sci U S A
Year 2003
Volume 100
Pages 13821-6
Authors Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K
Title X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.
Related PDB 1okt
Related UniProtKB Q8MU52
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE.
Medline ID
PubMed ID 12972411
Journal J Biol Chem
Year 2004
Volume 279
Pages 1336-42
Authors Perbandt M, Burmeister C, Walter RD, Betzel C, Liebau E
Title Native and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum.
Related PDB 1pa3 1q4j
Related UniProtKB Q8MU52
[10]
Resource
Comments
Medline ID
PubMed ID 16399390
Journal Methods Enzymol
Year 2005
Volume 401
Pages 241-53
Authors Deponte M, Becker K
Title Glutathione S-transferase from malarial parasites: structural and functional aspects.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 15888443
Journal J Biol Chem
Year 2005
Volume 280
Pages 26121-8
Authors Liebau E, De Maria F, Burmeister C, Perbandt M, Turella P, Antonini G, Federici G, Giansanti F, Stella L, Lo Bello M, Caccuri AM, Ricci G
Title Cooperativity and pseudo-cooperativity in the glutathione S-transferase from Plasmodium falciparum.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SELF-ASSOCIATION, AND MUTAGENESIS OF TYR-9; LYS-15; GLN-71; CYS-101 AND TYR-211.
Medline ID
PubMed ID 16385005
Journal Protein Sci
Year 2006
Volume 15
Pages 281-9
Authors Hiller N, Fritz-Wolf K, Deponte M, Wende W, Zimmermann H, Becker K
Title Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition.
Related PDB 2aaw
Related UniProtKB Q8MU52
[13]
Resource
Comments
Medline ID
PubMed ID 17941979
Journal BMC Struct Biol
Year 2007
Volume 7
Pages 67
Authors Tripathi T, Rahlfs S, Becker K, Bhakuni V
Title Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 19531494
Journal J Biol Chem
Year 2009
Volume 284
Pages 22133-9
Authors Liebau E, Dawood KF, Fabrini R, Fischer-Riepe L, Perbandt M, Stella L, Pedersen JZ, Bocedi A, Petrarca P, Federici G, Ricci G
Title Tetramerization and cooperativity in Plasmodium falciparum glutathione S-transferase are mediated by atypic loop 113-119.
Related PDB 3fr3 3fr6 3fr9 3frc
Related UniProtKB

Comments
There are various classes in GST enzymes. This enzyme is similar to none of the known GST classes (see [8]).
This enzyme family, GST, which catalyzes the conjugation of glutathione (GSH) to a variety of hydrophobic compounds, has an active-site that is composed of two binding sites: the G site, which binds reduced GSH, whilst the H site, which can bind a various kinds of compounds or substrates (see [8]). The H site of GST enzymes is more variable than the G site, due to a number of those substrates (see [8]).
Moreover, this enzyme has dual functions: one is conjugation of GSH to substrates, the other is peroxidase activity (see [11]).

Created Updated
2008-03-30 2015-01-13