Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione S-transferase 1

Gene

GST1

Organism
Onchocerca volvulus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421Glutathione1 Publication
Binding sitei73 – 731Glutathione1 Publication
Binding sitei77 – 771Glutathione1 Publication
Binding sitei85 – 851Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

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 1 (EC:2.5.1.18)
Gene namesi
Name:GST1
Synonyms:GSTA
OrganismiOnchocerca volvulus
Taxonomic identifieri6282 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeOnchocerca
ProteomesiUP000024404: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 235›235Glutathione S-transferase 1PRO_0000185969Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 469Combined sources
Helixi47 – 493Combined sources
Helixi50 – 5910Combined sources
Beta strandi64 – 685Combined sources
Helixi70 – 767Combined sources
Helixi77 – 793Combined sources
Beta strandi80 – 834Combined sources
Beta strandi87 – 904Combined sources
Beta strandi93 – 964Combined sources
Helixi98 – 10811Combined sources
Helixi116 – 14126Combined sources
Helixi145 – 15612Combined sources
Turni157 – 1593Combined sources
Helixi160 – 17213Combined sources
Beta strandi175 – 1773Combined sources
Helixi186 – 19712Combined sources
Helixi199 – 2013Combined sources
Helixi204 – 2063Combined sources
Helixi208 – 21912Combined sources
Helixi223 – 2297Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HNLX-ray2.00A/B11-235[»]
ProteinModelPortaliP46434.
SMRiP46434. Positions 34-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46434.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 11378GST N-terminalAdd
BLAST
Domaini115 – 235121GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 982Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

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]
PfamiPF14497. GST_C_3. 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: Fragment.

P46434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FITMNFVVEA ASSNANQAIT SENSIKPKGK LQPQMEKYTL TYFNGRGRAE
60 70 80 90 100
VIRLLFALAN VSYEDNRITR DEWKYLKPRT PFGHVPMLNV SGNVLGESHA
110 120 130 140 150
IELLLGGRFG LLGTNDWEEA KIMAVVLNID ELFQKLIPWT HEKNTTKKAE
160 170 180 190 200
LFRNLSESDV MPFLGRYEKF LKESTTGHIV GNKVSVADLT VFNMLMTLDD
210 220 230
EVKLEEYPQL ASFVNKIGQM PGIKEWIKKR PKTYF
Length:235
Mass (Da):26,838
Last modified:November 1, 1995 - v1
Checksum:iF28928E44102F63A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75029 mRNA. Translation: CAA52937.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75029 mRNA. Translation: CAA52937.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HNLX-ray2.00A/B11-235[»]
ProteinModelPortaliP46434.
SMRiP46434. Positions 34-235.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP46434.

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]
PfamiPF14497. GST_C_3. 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]
ProtoNetiSearch...

Publicationsi

  1. "Isolation, sequence and expression of an Onchocerca volvulus glutathione S-transferase cDNA."
    Liebau E., Walter R.D., Henkle-Duehrsen K.
    Mol. Biochem. Parasitol. 63:305-309(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus."
    Perbandt M., Hoppner J., Burmeister C., Luersen K., Betzel C., Liebau E.
    J. Mol. Biol. 377:501-511(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-235 IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

Entry informationi

Entry nameiGST1_ONCVO
AccessioniPrimary (citable) accession number: P46434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 4, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.