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P30114

- GST28_SCHHA

UniProt

P30114 - GST28_SCHHA

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Protein

Glutathione S-transferase class-mu 28 kDa isozyme

Gene
N/A
Organism
Schistosoma haematobium (Blood fluke)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication
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.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione
Binding sitei16 – 161Glutathione
Binding sitei53 – 531Glutathione; via amide nitrogen and carbonyl oxygen

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase class-mu 28 kDa isozyme (EC:2.5.1.18)
Short name:
GST 28
Alternative name(s):
Sh28GST
OrganismiSchistosoma haematobium (Blood fluke)
Taxonomic identifieri6185 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Glutathione S-transferase class-mu 28 kDa isozymePRO_0000185813Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117
Helixi18 – 269
Beta strandi32 – 354
Turni38 – 403
Helixi41 – 444
Helixi45 – 473
Helixi49 – 513
Beta strandi55 – 595
Beta strandi65 – 706
Helixi71 – 8111
Helixi89 – 11022
Turni111 – 1144
Helixi117 – 12812
Helixi131 – 14414
Beta strandi147 – 1526
Helixi158 – 17316
Turni175 – 1806
Helixi183 – 19513
Helixi197 – 20610

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OE7X-ray1.80A/B1-211[»]
1OE8X-ray1.65A/B1-211[»]
ProteinModelPortaliP30114.
SMRiP30114. Positions 4-211.

Miscellaneous databases

EvolutionaryTraceiP30114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8683GST N-terminalAdd
BLAST
Domaini88 – 211124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 455Glutathione binding
Regioni70 – 712Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30114-1 [UniParc]FASTAAdd to Basket

« Hide

MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG    50
GRLPAVKITD NHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYNVEKLIG 100
QVEDLEHEYH KTLMKPEEEK QKITKEILNG KVPVLLDIIC ESLKASTGKL 150
AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG KYPEIHKHRE NLLASSPRLA 200
KYLSDRAATP F 211
Length:211
Mass (Da):23,960
Last modified:April 1, 1993 - v1
Checksum:i954B2B60AA22E2C8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87800 Genomic DNA. Translation: AAA29893.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87800 Genomic DNA. Translation: AAA29893.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OE7 X-ray 1.80 A/B 1-211 [» ]
1OE8 X-ray 1.65 A/B 1-211 [» ]
ProteinModelPortali P30114.
SMRi P30114. Positions 4-211.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P30114.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Inter-species variation of schistosome 28-kDa glutathione S-transferases."
    Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P., Capron A.
    Mol. Biochem. Parasitol. 54:63-72(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium."
    Johnson K.A., Angelucci F., Bellelli A., Herve M., Fontaine J., Tsernoglou D., Capron A., Trottein F., Brunori M.
    Biochemistry 42:10084-10094(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiGST28_SCHHA
AccessioniPrimary (citable) accession number: P30114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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