eF-site ID 3gtu-ABCD PDB Code 3gtu Chain A, B, C, D click to enlarge Title LIGAND-FREE HETERODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M2-3 (EC 2.5.1.18), MONOCLINIC CRYSTAL FORM Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE Source Homo sapiens (Human) (GSTM3_HUMAN) Sequence A:  PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDY DRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIA RKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFE KLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAY DVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSS RFLPRPVFTKMAVWGNK B:  SCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGE APDYDRSQWLDVKFKLDLDFPNLPYLLDGKNKITQSNAIL RYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCYS SDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVD FLTYDILDQNRIFDPKCLDEFPNLKAFMCRFEALEKIAAY LQSDQFCKMPINNKMAQWGNKPVC C:  PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDY DRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIA RKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFE KLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAY DVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSS RFLPRPVFTKMAVWGNK D:  SCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGE APDYDRSQWLDVKFKLDLDFPNLPYLLDGKNKITQSNAIL RYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCYS SDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVD FLTYDILDQNRIFDPKCLDEFPNLKAFMCRFEALEKIAAY LQSDQFCKMPINNKMAQWGNKPVC Description Functional site 1) chain B residue 10 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 49 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 62 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 75 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 10 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 6) chain D residue 49 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 7) chain D residue 62 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 8) chain D residue 75 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P08515 source Swiss-Prot : SWS_FT_FI1 9) chain B residue 119 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 119 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 53 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 12) chain C residue 116 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 72 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 14) chain D residue 53 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 15) chain D residue 72 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 210 type SITE sequence K description Important for substrate specificity source Swiss-Prot : SWS_FT_FI4 17) chain C residue 210 type SITE sequence K description Important for substrate specificity source Swiss-Prot : SWS_FT_FI4 18) chain A residue 27 type MOD_RES sequence Y description Phosphoserine => ECO:0000250|UniProtKB:P08010 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 44 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:P08010 source Swiss-Prot : SWS_FT_FI5 20) chain C residue 27 type MOD_RES sequence Y description Phosphoserine => ECO:0000250|UniProtKB:P08010 source Swiss-Prot : SWS_FT_FI5 21) chain C residue 44 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:P08010 source Swiss-Prot : SWS_FT_FI5

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