eF-site ID 6gst-A PDB Code 6gst Chain A click to enlarge Title FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE Classification TRANSFERASE Compound MU CLASS GLUTATHIONE S-TRANSFERASE OF ISOENZYME 3-3 Source Rattus norvegicus (Rat) (GSTM1_RAT) Sequence A:  PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDY DRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLA RKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFE KQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAY DILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS RYLSTPIFSKLAQWSNK Description Functional site 1) chain A residue 6 type sequence Y description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 2) chain A residue 7 type sequence W description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 3) chain A residue 45 type sequence W description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 4) chain A residue 49 type sequence K description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 5) chain A residue 58 type sequence N description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 6) chain A residue 59 type sequence L description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 7) chain A residue 71 type sequence Q description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 8) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE GSH A 218 source : AC1 9) chain A residue 105 type sequence D description BINDING SITE FOR RESIDUE GSH B 218 source : AC2 10) chain A residue 50 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 59 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 72 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 7 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 43 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 116 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 67 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 205 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 210 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3

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