1V40,1PD2,2VCQ,3EE2


Conserved Protein Domain Family
GST_C_Sigma

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cd10295: GST_C_Sigma 
Click on image for an interactive view with Cn3D
C-terminal, alpha helical domain of Class Sigma Glutathione S-transferases
Glutathione S-transferase (GST) C-terminal domain family, Class Sigma; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation.
Statistics
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PSSM-Id: 198328
Aligned: 7 rows
Threshold Bit Score: 138.014
Created: 4-May-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interfacesubstrateN-terminal
Conserved site includes 14 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Comment:Residues from both N-terminal TRX-fold and C-terminal alpha helical domains form the dimer interface.
  • Structure:1PD2; Rattus norvegicus Prostaglandin D Synthase (class Sigma GST) dimer interface; contacts at 4A
    View structure with Cn3D
  • Citation:PMID 9323136
  • Structure:2VCQ; Human Prostaglandin D2 Synthase dimer interface; contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1     ## ### ### ##  #                                 ##  #                          
1V40_D     81 EMEQCHVDAIVDTLDDFMSCFPWaekkq-dvkeqMFNELLTynAPHLMQDLDTYLggrEWLIGmSVTWADFYWEICSTTL 159 human
1PD2_2     82 ELEQCQVDAVVDTLDDFMSLFPWaeenq-dlkerTFNDLLTrqAPHLLKDLDTYLgdkEWFIGnYVTWADFYWDICSTTL 160 Norway rat
2VCQ_A     82 EMEQCHVDAIVDTLDDFMSCFPWaekkqdvkeqmFNELLTYn-APHLMQDLDTYLggrEWLIGnSVTWADFYWEICSTTL 160 human
3EE2_A     82 EMEQCHVDAIVDTLDDFMSCFPWaekkqdvkeqmFNELLTYn-APHLMQDLDTYLggrEWLIGnSVTWADFYWEICSTTL 160 chimpanzee
CAA07005   82 PVEQALADAIVDTIDDFMMLFPWaeknqdvkekaFNDILTNk-APELLKDLDTFLgdkKWFVGkSVTWADFYWDVCSTTL 160 chicken
AAH53774   82 ELDEIRVDALIDTIDDFFSKFPWmdt-----ekaKKEFMEKs-SPQLLAYLEKTLgnnPWFVGdSATWADFFWDTCADSF 155 African clawed frog
AAQ76780   87 SLDMALVDSLVDHMDDLMKNLPFyekdeekkkkmIAEAMAGp-IKEGLKKLEKYVtedNVLVGkCITLADIDFQTGAEFL 165 Herdmania curvata
Feature 1                            
1V40_D    160 Lvfkpd--lldnhPRLVTLRKKV 180 human
1PD2_2    161 Lvlkpd--llgiyPRLVSLRNKV 181 Norway rat
2VCQ_A    161 Lvfkpd--lldnhPRLVTLRKKV 181 human
3EE2_A    161 Lvfkpd--lldnhPRLVTLRKKV 181 chimpanzee
CAA07005  161 Lsykad--ladkyPRLLALRDRV 181 chicken
AAH53774  156 Esyvpg--fakdyPKLLALKERV 176 African clawed frog
AAQ76780  166 IsfsgdenvlkstPKLQAVYDKV 188 Herdmania curvata

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