eF-site ID 11gs-B PDB Code 11gs Chain B click to enlarge Title Glutathione s-transferase complexed with ethacrynic acid-glutathione conjugate (form ii) Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE Source Homo sapiens (Human) (GTP_HUMAN) Sequence B:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL PINGNGKQ Description Functional site 1) chain B residue 98 type sequence D description BINDING SITE FOR RESIDUE GSH A 210 source : AC1 2) chain B residue 171 type sequence D description BINDING SITE FOR RESIDUE MES A 212 source : AC3 3) chain B residue 7 type sequence Y description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 4) chain B residue 13 type sequence R description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 5) chain B residue 38 type sequence W description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 6) chain B residue 44 type sequence K description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 7) chain B residue 50 type sequence G description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 8) chain B residue 51 type sequence Q description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 9) chain B residue 52 type sequence L description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 10) chain B residue 53 type sequence P description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 11) chain B residue 64 type sequence Q description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 12) chain B residue 65 type sequence S description BINDING SITE FOR RESIDUE GSH B 210 source : AC4 13) chain B residue 7 type sequence Y description BINDING SITE FOR RESIDUE EAA B 211 source : AC5 14) chain B residue 104 type sequence I description BINDING SITE FOR RESIDUE EAA B 211 source : AC5 15) chain B residue 108 type sequence Y description BINDING SITE FOR RESIDUE EAA B 211 source : AC5 16) chain B residue 205 type sequence G description BINDING SITE FOR RESIDUE EAA B 211 source : AC5 17) chain B residue 22 type sequence A description BINDING SITE FOR RESIDUE MES B 212 source : AC6 18) chain B residue 28 type sequence W description BINDING SITE FOR RESIDUE MES B 212 source : AC6 19) chain B residue 30 type sequence E description BINDING SITE FOR RESIDUE MES B 212 source : AC6 20) chain B residue 197 type sequence E description BINDING SITE FOR RESIDUE MES B 212 source : AC6 21) chain B residue 3 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 198 type MOD_RES sequence Y description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 61 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 115 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 44 type BINDING sequence K description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 51 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 64 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 7 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 13 type BINDING sequence R description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 38 type BINDING sequence W description BINDING => ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

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