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257  structures 4920  species 0  interactions 22286  sequences 288  architectures

Family: GST_C_2 (PF13410)

Summary: Glutathione S-transferase, C-terminal domain

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This is the Wikipedia entry entitled "Glutathione S-transferase, C-terminal domain". More...

Glutathione S-transferase, C-terminal domain Edit Wikipedia article

Glutathione S-transferase, C-terminal domain
OPM superfamily139
OPM protein1z9h

Glutathione S-transferase, C-terminal domain is a structural domain of glutathione S-transferase (GST).

GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants.

The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.

Biological function and classification

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 cephalopods is also a GST[1][2][3][4].

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[5][6]. GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.


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. Each monomer is composed of a distinct N-terminal sub-domain, which adopts the thioredoxin fold, and a C-terminal all-helical sub-domain. This entry is the C-terminal domain.

Human proteins containing this domain



  1. ^ Armstrong RN (1997). "Structure, catalytic mechanism, and evolution of the glutathione transferases". Chem. Res. Toxicol. 10 (1): 2–18. PMID 9074797.
  2. ^ Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J (2000). "Identification, characterization, and crystal structure of the Omega class glutathione transferases". J. Biol. Chem. 275 (32): 24798–24806. PMID 10783391. {{cite journal}}: line feed character in |author= at position 34 (help)CS1 maint: multiple names: authors list (link)
  3. ^ Board P, Chelvanayagam G, Dulhunty A, Gage P, Curtis S (2001). "The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator". J. Biol. Chem. 276 (5): 3319–3323. PMID 11035031.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Eaton DL, Bammler TK (1999). "Concise review of the glutathione S-transferases and their significance to toxicology". Toxicol. Sci. 49 (2): 156–164. PMID 10416260.
  5. ^ Parker MW, Board PG, Polekhina G, Blackburn AC (2001). "Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity". Biochemistry. 40 (6): 1567–1576. PMID 11327815.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Vuilleumier S (1997). "Bacterial glutathione S-transferases: what are they good for?". J. Bacteriol. 179 (5): 1431–1441. PMID 9045797.

Further reading

  • [1]. Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K; J Mol Biol 1998;281:135-147. PMID 9680481
  • [2]. Plant glutathione transferases. Dixon DP, Lapthorn A, Edwards R; Genome Biol 2002;3:REVIEWS3004. PMID 11897031

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, C-terminal domain Provide feedback

This domain is closely related to PF00043.

Internal database links

This tab holds annotation information from the InterPro database.

No InterPro data for this Pfam family.

Domain organisation

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

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Pfam Clan

This family is a member of clan GST_C (CL0497), which has the following description:

This clan represents the C-terminal domain of Glutathione S-transferase.

The clan contains the following 8 members:

Glutaredoxin2_C GST_C GST_C_2 GST_C_3 GST_C_4 GST_C_5 GST_C_6 Tom37_C


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.

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Representative proteomes UniProt

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

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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.

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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: 135
Number in full: 22286
Average length of the domain: 86.8 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 30.14 %

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 24.9 24.9
Trusted cut-off 24.9 24.9
Noise cut-off 24.8 24.8
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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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_C_2 domain has been found. There are 257 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
A0A044V0V1 View 3D Structure Click here
A0A077Z4J6 View 3D Structure Click here
A0A0D2DJ78 View 3D Structure Click here
A0A0D2DRF9 View 3D Structure Click here
A0A0D2DYE2 View 3D Structure Click here
A0A0D2F6P4 View 3D Structure Click here
A0A0D2G5Q7 View 3D Structure Click here
A0A0D2GAN7 View 3D Structure Click here
A0A0D2GET0 View 3D Structure Click here
A0A0D2GP32 View 3D Structure Click here
A0A0D2GXC7 View 3D Structure Click here
A0A0D2GXU1 View 3D Structure Click here
A0A0D2GYN8 View 3D Structure Click here
A0A0D2H1X2 View 3D Structure Click here
A0A0D2H266 View 3D Structure Click here
A0A0H3GQD2 View 3D Structure Click here
A0A0H3GVR7 View 3D Structure Click here
A0A0H3GYT0 View 3D Structure Click here
A0A0H3H341 View 3D Structure Click here
A0A0H5SC56 View 3D Structure Click here
A0A0K0DV75 View 3D Structure Click here
A0A0K0E470 View 3D Structure Click here
A0A0K0JH04 View 3D Structure Click here
A0A0R0ENV1 View 3D Structure Click here
A0A0R0ENV4 View 3D Structure Click here
A0A0R0INI5 View 3D Structure Click here
A0A0R4IRJ8 View 3D Structure Click here
A0A175VYI3 View 3D Structure Click here
A0A175VZ60 View 3D Structure Click here
A0A175VZ73 View 3D Structure Click here
A0A175WCH8 View 3D Structure Click here
A0A175WE91 View 3D Structure Click here
A0A1C1C879 View 3D Structure Click here
A0A1C1CDQ9 View 3D Structure Click here
A0A1C1CJ04 View 3D Structure Click here
A0A1C1CJJ2 View 3D Structure Click here
A0A1C1CL53 View 3D Structure Click here
A0A1C1CQ12 View 3D Structure Click here
A0A1C1CT31 View 3D Structure Click here
A0A1C1CTL5 View 3D Structure Click here