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(-) Description

Title :  CRYSTAL STRUCTURE OF GLUTATHIONE TRANSFERASE DMGSTD1 FROM DROSOPHILA MELANOGASTER, IN COMPLEX WITH GLUTATHIONE
 
Authors :  J. Wongsantichon, R. C. Robinson, A. J. Ketterman
Date :  24 Mar 10  (Deposition) - 30 Mar 11  (Release) - 08 Jul 15  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.80
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (2x)
Keywords :  Protein-Substrate Complex, Transferase (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  J. Wongsantichon, R. C. Robinson, A. J. Ketterman
Structural Evidence For Conformational Changes Of Delta Class Glutathione Transferases After Ligand Binding
Arch. Biochem. Biophys. V. 521 77 2012
PubMed-ID: 22475449  |  Reference-DOI: 10.1016/J.ABB.2012.03.023

(-) Compounds

Molecule 1 - GLUTATHIONE S-TRANSFERASE 1-1
    ChainsA
    EC Number2.5.1.18
    EngineeredYES
    Expression SystemESCHERICHIA COLI
    Expression System PlasmidPET3A
    Expression System StrainBL21(DE3)PLYSS
    Expression System Taxid469008
    Expression System Vector TypePLASMID
    GeneGSTD1
    Organism CommonFRUIT FLY
    Organism ScientificDROSOPHILA MELANOGASTER
    Organism Taxid7227
    SynonymGLUTATHIONE TRANSFERASE DMGSTD1, GST CLASS-THETA

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit A
Biological Unit 1 (2x)A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 1)

Asymmetric Unit (1, 1)
No.NameCountTypeFull Name
1GSH1Ligand/IonGLUTATHIONE
Biological Unit 1 (1, 2)
No.NameCountTypeFull Name
1GSH2Ligand/IonGLUTATHIONE

(-) Sites  (1, 1)

Asymmetric Unit (1, 1)
No.NameEvidenceResiduesDescription
1AC1SOFTWARESER A:10 , PRO A:12 , HIS A:39 , HIS A:51 , THR A:52 , ILE A:53 , PRO A:54 , GLU A:65 , SER A:66 , ARG A:67 , MET A:102 , HOH A:233 , HOH A:234 , HOH A:238 , HOH A:253 , HOH A:270 , HOH A:294BINDING SITE FOR RESIDUE GSH A 210

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 3MAK)

(-) Cis Peptide Bonds  (1, 1)

Asymmetric Unit
No.Residues
1Ile A:53 -Pro A:54

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 3MAK)

(-) PROSITE Motifs  (1, 1)

Asymmetric Unit (1, 1)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1GST_CTERPS50405 Soluble glutathione S-transferase C-terminal domain profile.GSTD1_DROME87-208  1A:87-208
Biological Unit 1 (1, 2)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1GST_CTERPS50405 Soluble glutathione S-transferase C-terminal domain profile.GSTD1_DROME87-208  2A:87-208

(-) Exons   (0, 0)

(no "Exon" information available for 3MAK)

(-) Sequences/Alignments

Asymmetric Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:208
 aligned with GSTD1_DROME | P20432 from UniProtKB/Swiss-Prot  Length:209

    Alignment length:208
                                    11        21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201        
          GSTD1_DROME     2 VDFYYLPGSSPCRSVIMTAKAVGVELNKKLLNLQAGEHLKPEFLKINPQHTIPTLVDNGFALWESRAIQVYLVEKYGKTDSLYPKCPKKRAVINQRLYFDMGTLYQSFANYYYPQVFAKAPADPEAFKKIEAAFEFLNTFLEGQDYAAGDSLTVADIALVATVSTFEVAKFEISKYANVNRWYENAKKVTPGWEENWAGCLEFKKYFE 209
               SCOP domains d3maka1 A:2-85 automated matches                                                    d3maka2 A:86-209 automated matches                                                                                           SCOP domains
               CATH domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .eeee...hhhhhhhhhhhhhhh...eeee.hhhhhhhhhhhhhh........eeee..eeeehhhhhhhhhhhhhh........hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh...hhhhhhhhhhhhhhhhhhh...........hhhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhhh Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE -------------------------------------------------------------------------------------GST_CTER  PDB: A:87-208 UniProt: 87-208                                                                                   - PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3mak A   2 VDFYYLPGSSPCRSVIMTAKAVGVELNKKLLNLQAGEHLKPEFLKINPQHTIPTLVDNGFALWESRAIQVYLVEKYGKTDSLYPKCPKKRAVINQRLYFDMGTLYQSFANYYYPQVFAKAPADPEAFKKIEAAFEFLNTFLEGQDYAAGDSLTVADIALVATVSTFEVAKFEISKYANVNRWYENAKKVTPGWEENWAGCLEFKKYFE 209
                                    11        21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201        

   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (2, 2)

Asymmetric Unit

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 3MAK)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 3MAK)

(-) Gene Ontology  (9, 9)

Asymmetric Unit(hide GO term definitions)
Chain A   (GSTD1_DROME | P20432)
molecular function
    GO:0018833    DDT-dehydrochlorinase activity    Catalysis of the reaction: 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride + H(+).
    GO:0004602    glutathione peroxidase activity    Catalysis of the reaction: 2 glutathione + hydrogen peroxide = oxidized glutathione + 2 H2O.
    GO:0004364    glutathione transferase activity    Catalysis of the reaction: R-X + glutathione = H-X + R-S-glutathione. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group.
    GO:0016829    lyase activity    Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
    GO:0016740    transferase activity    Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
biological process
    GO:0098869    cellular oxidant detoxification    Any process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide.
    GO:0006749    glutathione metabolic process    The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.
    GO:0009636    response to toxic substance    Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus.
cellular component
    GO:0005737    cytoplasm    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        GSTD1_DROME | P204323ein

(-) Related Entries Specified in the PDB File

3f6f DIFFERENT MEMBER OF DELTA CLASS GLUTATHIONE TRANSFERASES IN DROSOPHILA MELANOGASTER
3gh6 DIFFERENT MEMBER OF DELTA CLASS GLUTATHIONE TRANSFERASES IN DROSOPHILA MELANOGASTER