eF-site ID 1mtc-B PDB Code 1mtc Chain B click to enlarge Title GLUTATHIONE TRANSFERASE MUTANT Y115F Classification TRANSFERASE Compound Glutathione S-transferase YB1 Source Rattus norvegicus (Rat) (GSTM1_RAT) Sequence B:  PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDY DRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLA RKHHLCGETEEERIRADIVENQVMDNRMQLIMLCFNPDFE KQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAY DILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS RYLSTPIFSKLAQWSNK Description Functional site 1) chain B residue 105 type sequence D description BINDING SITE FOR RESIDUE GPR A 5218 source : AC1 2) chain B residue 6 type sequence Y description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 3) chain B residue 7 type sequence W description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 4) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 5) chain B residue 12 type sequence L description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 6) chain B residue 45 type sequence W description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 7) chain B residue 49 type sequence K description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 8) chain B residue 58 type sequence N description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 9) chain B residue 59 type sequence L description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 10) chain B residue 71 type sequence Q description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 11) chain B residue 72 type sequence S description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 12) chain B residue 104 type sequence M description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 13) chain B residue 111 type sequence I description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 14) chain B residue 115 type sequence F description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 15) chain B residue 209 type sequence S description BINDING SITE FOR RESIDUE GPR B 6218 source : AC2 16) chain B residue 72 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 7 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 43 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 50 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 59 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 116 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 67 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 205 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 210 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3

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