eF-site ID 6mhc-A PDB Code 6mhc Chain A click to enlarge Title Glutathione S-Transferase Omega 1 bound to covalent inhibitor 37 Classification Transferase/Transferase Inhibitor Compound Glutathione S-transferase omega-1 Source (GSTO1_HUMAN) Sequence A:  SNAMSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAER TRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLEN SQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMIL ELFSKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVL TNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTP KLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEAC DYGL Description Functional site 1) chain A residue 29 type sequence M description binding site for residue JRM A 301 source : AC1 2) chain A residue 32 type sequence C description binding site for residue JRM A 301 source : AC1 3) chain A residue 56 type sequence L description binding site for residue JRM A 301 source : AC1 4) chain A residue 72 type sequence V description binding site for residue JRM A 301 source : AC1 5) chain A residue 128 type sequence G description binding site for residue JRM A 301 source : AC1 6) chain A residue 132 type sequence R description binding site for residue JRM A 301 source : AC1 7) chain A residue 229 type sequence Y description binding site for residue JRM A 301 source : AC1 8) chain A residue 230 type sequence L description binding site for residue JRM A 301 source : AC1 9) chain A residue 56 type sequence L description binding site for residue DMS A 302 source : AC2 10) chain A residue 59 type sequence K description binding site for residue DMS A 302 source : AC2 11) chain A residue 71 type sequence L description binding site for residue DMS A 302 source : AC2 12) chain A residue 229 type sequence Y description binding site for residue DMS A 302 source : AC2 13) chain A residue 43 type sequence K description binding site for residue PEG A 303 source : AC3 14) chain A residue 211 type sequence T description binding site for residue PEG A 303 source : AC3 15) chain A residue 34 type sequence F description binding site for residue MES A 304 source : AC4 16) chain A residue 85 type sequence E description binding site for residue MES A 304 source : AC4 17) chain A residue 86 type sequence S description binding site for residue MES A 304 source : AC4 18) chain A residue 118 type sequence E description binding site for residue MES B 304 source : AC7 19) chain A residue 32 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:10783391 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 59 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 72 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 85 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 57 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 143 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 148 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 152 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 129 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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