eF-site ID 5fwg-A PDB Code 5fwg Chain A click to enlarge Title TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE Classification TRANSFERASE Compound TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE MU CLASS Source Rattus norvegicus (Rat) (GSTM1_RAT) Sequence A:  PMILGYXNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDY DRSQXLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLA RKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFE KQKPEFLKTIPEKMKLYSEFLGKRPXFAGDKVTYVDFLAY DILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS RYLSTPIFSKLAQXSNK Description Functional site 1) chain A residue 6 type sequence Y description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 2) chain A residue 7 type sequence X description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 3) chain A residue 9 type sequence V description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 4) chain A residue 12 type sequence L description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 5) chain A residue 111 type sequence I description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 6) chain A residue 115 type sequence Y description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 7) chain A residue 209 type sequence S description ACTIVE SITE DEFINED LARGELY BY THESE RESIDUES. source : GPS 8) chain A residue 6 type sequence Y description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 9) chain A residue 7 type sequence X description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 10) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 11) chain A residue 12 type sequence L description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 12) chain A residue 45 type sequence X description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 13) chain A residue 49 type sequence K description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 14) chain A residue 58 type sequence N description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 15) chain A residue 59 type sequence L description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 16) chain A residue 60 type sequence P description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 17) chain A residue 71 type sequence Q description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 18) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 19) chain A residue 104 type sequence M description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 20) chain A residue 111 type sequence I description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 21) chain A residue 209 type sequence S description BINDING SITE FOR RESIDUE GPR A 218 source : AC1 22) chain A residue 105 type sequence D description BINDING SITE FOR RESIDUE GPR B 218 source : AC2 23) chain A residue 50 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 59 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 72 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 7 type BINDING sequence X description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 43 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 116 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 67 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 205 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI3 31) 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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