NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0166-6851(92)90095-2; PubMed=1518533 [NCBI, ExPASy, EBI, Israel, Japan]
Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P., Capron A.;
"Inter-species variation of schistosome 28-kDa glutathione S-transferases.";
Mol. Biochem. Parasitol. 54:63-72(1992).

[2]

X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/j.jmb.2006.05.040; PubMed=16777141 [NCBI, ExPASy, EBI, Israel, Japan]
Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M., Miele A.E., Trottein F., Brunori M., Bellelli A.;
"Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography.";
J. Mol. Biol. 360:678-689(2006).

Comments

FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the GST superfamily. Mu family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M87799; AAA29892.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

2C80; X-ray; 2.30 A; A/B=1-211.	[ExPASy / RCSB / EBI]
2C8U; X-ray; 2.00 A; A/B=1-211.	[ExPASy / RCSB / EBI]
2CA8; X-ray; 2.49 A; A=1-211.	[ExPASy / RCSB / EBI]
2CAI; X-ray; 2.26 A; A/B=1-211.	[ExPASy / RCSB / EBI]
2CAQ; X-ray; 2.00 A; A=1-211.	[ExPASy / RCSB / EBI]
2F8F; X-ray; 2.10 A; A/B=1-211.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2C80; -.
2C8U; -.
2CA8; -.
2CAI; -.
2CAQ; -.
2F8F; -.

ModBase

P30113.

Ontologies

GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P30113.

Other

DrugBank

DB00143; Glutathione.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 211`	`211`	`Glutathione S-transferase class-mu 28 kDa isozyme.`	`PRO_0000185812`
`DOMAIN`	`4 86`	`83`	`GST N-terminal.`
`DOMAIN`	`88 211`	`124`	`GST C-terminal.`
`ACT_SITE`	`10 10`
`STRAND`	`5 11`	`7`
`TURN`	`13 17`	`5`
`HELIX`	`18 27`	`10`
`STRAND`	`32 35`	`4`
`TURN`	`38 40`	`3`
`TURN`	`42 44`	`3`
`HELIX`	`45 47`	`3`
`STRAND`	`53 59`	`7`
`STRAND`	`65 69`	`5`
`HELIX`	`71 81`	`11`
`HELIX`	`89 110`	`22`
`HELIX`	`117 129`	`13`
`HELIX`	`131 144`	`14`
`STRAND`	`147 152`	`6`
`HELIX`	`158 173`	`16`
`HELIX`	`183 195`	`13`
`HELIX`	`197 203`	`7`

Sequence information

Length: 211 AA [This is the length of the unprocessed precursor]

Molecular weight: 23898 Da [This is the MW of the unprocessed precursor]

CRC64: 9B9F1358710D3C76 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG GRLPAVKITD 

        70         80         90        100        110        120 
NHGHVKWMVE SLAIARYMAK KHHMMGGTEE EYYNVEKLIG QAEDLEHEYY KTLMKPEEEK 

       130        140        150        160        170        180 
QKIIKEILNG KVPVLLDIIC ESLKASTGKL AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG 

       190        200        210 
KYPEIHKHRE NLLASSPRLA KYLSDRAATP F

P30113 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools