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175  structures 4319  species 0  interactions 11425  sequences 156  architectures

Family: GST_N_2 (PF13409)

Summary: Glutathione S-transferase, N-terminal domain

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This is the Wikipedia entry entitled "Glutathione S-transferase". More...

Glutathione S-transferase Edit Wikipedia article

The Glutathione S-transferase (GST) family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins which are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic.

Families of GST

  • Mammalian
    • Alpha
      • A1-1
      • A2-2
      • A3-3
      • A4-4
      • hGST5.8 (putative)
    • Mu
      • M1-1
    • Pi
      • P1-1
    • Theta
    • Zeta
    • Omega

Structure of GSTs

Mammalian cytosolic GSTs are homodimeric, and the monomers are in the range of 22-29 kDa. They are active over a wide variety of substrates with considerable overlap.

GSTs and Biotransformation

Glutathione S-transferases are considered, among several others, to contribute to the phase II biotransformation of xenobiotics. Drugs, poisons, and other compounds not traditionally listed in either groups are usually somewhat modified by the phase I and/or phase II mechanisms, and finally exreted from the body. GSTs contribute to this type of metabolism by conjugating these compounds (often electrophilic and somewhat lipophilic in nature) with reduced glutathione to facilitate dissolution in the aqueous cellular and extracelluar media, and from there, out of the body.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Glutathione S-transferase, N-terminal domain Provide feedback

This family is closely related to PF02798.

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004045

In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic compounds by catalysing their conjugation to glutathione. The GST domain is also found in S-crystallins from squid, and proteins with no known GST activity, such as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins, which include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of Cephalopoda is also a GST [ PUBMED:9074797 , PUBMED:10783391 , PUBMED:11035031 , PUBMED:10416260 ].

Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins, like the stringent starvation proteins, also belong to the GST family [ PUBMED:11327815 , PUBMED:9045797 ]. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.

Soluble GSTs activate glutathione (GSH) to GS-. In many GSTs, this is accomplished by a Tyr at H-bonding distance from the sulphur of GSH. These enzymes catalyse nucleophilic attack by reduced glutathione (GSH) on nonpolar compounds that contain an electrophilic carbon, nitrogen, or sulphur atom [ PUBMED:16399376 ].

Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold, with each monomer composed of two distinct domains [ PUBMED:12211029 ]. The N-terminal domain forms a thioredoxin-like fold that binds the glutathione moiety, while the C-terminal domain contains several hydrophobic alpha-helices that specifically bind hydrophobic substrates.

This entry represents the N-terminal domain of GST.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Jackhmmer:A3PFR8
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 149
Number in full: 11425
Average length of the domain: 83.8 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 27.6 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 25.0
Noise cut-off 24.9 24.9
Model length: 70
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GST_N_2 domain has been found. There are 175 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0D2DRF9 View 3D Structure Click here
A0A0D2E4M1 View 3D Structure Click here
A0A0D2F0M3 View 3D Structure Click here
A0A0D2F4N6 View 3D Structure Click here
A0A0D2F6P4 View 3D Structure Click here
A0A0D2G5Q7 View 3D Structure Click here
A0A0D2GXC7 View 3D Structure Click here
A0A0D2GYN8 View 3D Structure Click here
A0A0D2H1X2 View 3D Structure Click here
A0A0D2H448 View 3D Structure Click here
A0A0H3GYT0 View 3D Structure Click here
A0A0R4IRJ8 View 3D Structure Click here
A0A175VYI3 View 3D Structure Click here
A0A175VZ60 View 3D Structure Click here
A0A175W4G8 View 3D Structure Click here
A0A175W6F0 View 3D Structure Click here
A0A175WCH8 View 3D Structure Click here
A0A175WD84 View 3D Structure Click here
A0A1C1C879 View 3D Structure Click here
A0A1C1CAY4 View 3D Structure Click here
A0A1C1CBB1 View 3D Structure Click here
A0A1C1CDQ9 View 3D Structure Click here
A0A1C1CJ04 View 3D Structure Click here
A0A1C1CJJ2 View 3D Structure Click here
A0A1C1CY86 View 3D Structure Click here
A0A1C1D1P9 View 3D Structure Click here
A0A1C1D2L9 View 3D Structure Click here
A0A1D6FAS6 View 3D Structure Click here
A0A1D6J5Y1 View 3D Structure Click here
A0A1D6JIJ3 View 3D Structure Click here
A0A1D6KVK8 View 3D Structure Click here
A0A1D6L691 View 3D Structure Click here
A0A1D6LL55 View 3D Structure Click here
A0A1D6M100 View 3D Structure Click here
A0A1D6MQD0 View 3D Structure Click here
A0A1D6MTI0 View 3D Structure Click here
A0A1D6MTI1 View 3D Structure Click here
A0A1D6QEA8 View 3D Structure Click here
A0A1D6QMM9 View 3D Structure Click here
A0A1D8PS56 View 3D Structure Click here