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P46427

- GSTP_ONCVO

UniProt

P46427 - GSTP_ONCVO

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Protein

Glutathione S-transferase 2

Gene
GST2
Organism
Onchocerca volvulus
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Appears to play a central role in the parasite detoxification system.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Glutathione
Binding sitei42 – 421Glutathione By similarity

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 2 (EC:2.5.1.18)
Alternative name(s):
GST class-pi
Gene namesi
Name:GST2
OrganismiOnchocerca volvulus
Taxonomic identifieri6282 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeOnchocerca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208Glutathione S-transferase 2PRO_0000185914Add
BLAST

Expressioni

Tissue specificityi

Hypodermis, wall of the seminal receptacle and spermatozoa of adult worms.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Helixi12 – 143
Helixi15 – 239
Beta strandi29 – 335
Helixi35 – 373
Turni39 – 413
Helixi42 – 443
Beta strandi52 – 554
Beta strandi58 – 625
Helixi63 – 7311
Helixi81 – 10727
Helixi109 – 11911
Helixi121 – 13212
Turni133 – 1353
Helixi136 – 1383
Beta strandi139 – 1413
Beta strandi144 – 1463
Helixi149 – 16416
Turni166 – 1716
Helixi173 – 18311
Helixi186 – 19712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU7X-ray1.50A/B1-208[»]
1TU8X-ray1.80A/B/C/D1-208[»]
ProteinModelPortaliP46427.
SMRiP46427. Positions 1-208.

Miscellaneous databases

EvolutionaryTraceiP46427.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7878GST N-terminalAdd
BLAST
Domaini80 – 200121GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 502Glutathione binding
Regioni62 – 632Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Pi 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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46427-1 [UniParc]FASTAAdd to Basket

« Hide

MSYKLTYFSI RGLAEPIRLF LVDQDIKFID DRIAKDDFSS IKSQFQFGQL    50
PCLYDGDQQI VQSGAILRHL ARKYNLNGEN EMETTYIDMF CEGVRDLHVK 100
YTRMIYMAYE TEKDPYIKSI LPGELAKFEK LLATRGNGRN LILGDKISYA 150
DYALFEELDV HQILDPHCLD KFPLLKAFHQ RMKDRPKLKE YCEKRDAAKV 200
PVNGNGKQ 208
Length:208
Mass (Da):24,232
Last modified:November 1, 1995 - v1
Checksum:iD3A76450AE7A1321
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L28771 mRNA. Translation: AAA53575.1.
X77393 mRNA. Translation: CAA54568.1.
PIRiS41933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L28771 mRNA. Translation: AAA53575.1 .
X77393 mRNA. Translation: CAA54568.1 .
PIRi S41933.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TU7 X-ray 1.50 A/B 1-208 [» ]
1TU8 X-ray 1.80 A/B/C/D 1-208 [» ]
ProteinModelPortali P46427.
SMRi P46427. Positions 1-208.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P46427.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01268. GSTRNSFRASEP.
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. "Molecular characterisation and localisation of an Onchocerca volvulus pi-class glutathione S-transferase."
    Salinas G., Braun G., Taylor D.W.
    Mol. Biochem. Parasitol. 66:1-9(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Guatemala.
  2. "Onchocerca volvulus: isolation and sequence of a second glutathione S-transferase cDNA."
    Liebau E., Walter R.D., Henkle-Duehrsen K.
    Exp. Parasitol. 79:68-71(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus."
    Perbandt M., Hoppner J., Betzel C., Walter R.D., Liebau E.
    J. Biol. Chem. 280:12630-12636(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE, SUBUNIT.

Entry informationi

Entry nameiGSTP_ONCVO
AccessioniPrimary (citable) accession number: P46427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 65 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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