eF-site ID 1gul-ABCDEFGH PDB Code 1gul Chain A, B, C, D, E, F, G, H click to enlarge Title HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Glutathione S-transferase A4 Source Homo sapiens (Human) (GSTA4_HUMAN) Sequence A:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF B:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF C:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF D:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF E:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF F:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF G:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF H:  RPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYK LQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFG KNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVN MAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQT ILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSK KKPPPDEIYVRTVYNIF Description Functional site 1) chain A residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTA 2) chain A residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTA 3) chain A residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTA 4) chain A residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTA 5) chain A residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTA 6) chain A residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTA 7) chain A residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTA 8) chain A residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTA 9) chain A residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTA 10) chain A residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTA 11) chain A residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTA 12) chain A residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 13) chain A residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 14) chain A residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 15) chain A residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 16) chain A residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 17) chain A residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 18) chain A residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 19) chain A residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTA 20) chain B residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTB 21) chain B residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTB 22) chain B residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTB 23) chain B residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTB 24) chain B residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTB 25) chain B residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTB 26) chain B residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTB 27) chain B residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTB 28) chain B residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTB 29) chain B residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTB 30) chain B residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTB 31) chain B residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 32) chain B residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 33) chain B residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 34) chain B residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 35) chain B residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 36) chain B residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 37) chain B residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 38) chain B residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTB 39) chain C residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTC 40) chain C residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTC 41) chain C residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTC 42) chain C residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTC 43) chain C residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTC 44) chain C residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTC 45) chain C residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTC 46) chain C residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTC 47) chain C residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTC 48) chain C residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTC 49) chain C residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTC 50) chain C residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 51) chain C residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 52) chain C residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 53) chain C residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 54) chain C residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 55) chain C residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 56) chain C residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 57) chain C residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTC 58) chain D residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTD 59) chain D residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTD 60) chain D residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTD 61) chain D residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTD 62) chain D residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTD 63) chain D residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTD 64) chain D residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTD 65) chain D residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTD 66) chain D residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTD 67) chain D residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTD 68) chain D residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTD 69) chain D residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 70) chain D residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 71) chain D residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 72) chain D residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 73) chain D residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 74) chain D residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 75) chain D residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 76) chain D residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTD 77) chain E residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTE 78) chain E residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTE 79) chain E residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTE 80) chain E residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTE 81) chain E residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTE 82) chain E residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTE 83) chain E residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTE 84) chain E residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTE 85) chain E residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTE 86) chain E residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTE 87) chain E residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTE 88) chain E residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 89) chain E residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 90) chain E residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 91) chain E residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 92) chain E residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 93) chain E residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 94) chain E residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 95) chain E residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTE 96) chain F residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTF 97) chain F residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTF 98) chain F residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTF 99) chain F residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTF 100) chain F residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTF 101) chain F residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTF 102) chain F residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTF 103) chain F residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTF 104) chain F residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTF 105) chain F residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTF 106) chain F residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTF 107) chain F residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTF 108) chain G residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTG 109) chain G residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTG 110) chain G residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTG 111) chain G residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTG 112) chain G residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTG 113) chain G residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTG 114) chain G residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTG 115) chain G residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTG 116) chain G residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTG 117) chain G residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTG 118) chain G residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTG 119) chain G residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 120) chain G residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 121) chain G residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 122) chain G residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 123) chain G residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 124) chain G residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 125) chain G residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 126) chain G residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTG 127) chain H residue 9 type sequence Y description GLUTATHIONE BINDING SITE. source : GTH 128) chain H residue 15 type sequence R description GLUTATHIONE BINDING SITE. source : GTH 129) chain H residue 41 type sequence L description GLUTATHIONE BINDING SITE. source : GTH 130) chain H residue 45 type sequence Q description GLUTATHIONE BINDING SITE. source : GTH 131) chain H residue 54 type sequence Q description GLUTATHIONE BINDING SITE. source : GTH 132) chain H residue 55 type sequence V description GLUTATHIONE BINDING SITE. source : GTH 133) chain H residue 67 type sequence Q description GLUTATHIONE BINDING SITE. source : GTH 134) chain H residue 68 type sequence T description GLUTATHIONE BINDING SITE. source : GTH 135) chain H residue 101 type sequence D description GLUTATHIONE BINDING SITE. source : GTH 136) chain H residue 131 type sequence R description GLUTATHIONE BINDING SITE. source : GTH 137) chain H residue 220 type sequence F description GLUTATHIONE BINDING SITE. source : GTH 138) chain H residue 14 type sequence G description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 139) chain H residue 104 type sequence E description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 140) chain H residue 107 type sequence I description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 141) chain H residue 108 type sequence M description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 142) chain H residue 111 type sequence F description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 143) chain H residue 212 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 144) chain H residue 216 type sequence V description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 145) chain H residue 217 type sequence Y description ELECTROPHILIC SUBSTRATE BINDING SITE. source : HTH 146) chain A residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 147) chain E residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 148) chain F residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 149) chain F residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 150) chain G residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 151) chain G residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 152) chain H residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 153) chain H residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 154) chain A residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 155) chain B residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 156) chain B residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 157) chain C residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 158) chain C residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 159) chain D residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 160) chain D residue 67 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 161) chain E residue 9 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P13745 source Swiss-Prot : SWS_FT_FI1 162) chain A residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 163) chain B residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 164) chain C residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 165) chain D residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 166) chain E residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 167) chain F residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 168) chain G residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 169) chain H residue 54 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30711 source Swiss-Prot : SWS_FT_FI2 170) chain A residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 171) chain B residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 172) chain C residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 173) chain D residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 174) chain E residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 175) chain F residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 176) chain G residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 177) chain H residue 212 type BINDING sequence Y description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI3

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