eF-site ID 3gss-B PDB Code 3gss Chain B click to enlarge Title HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE Classification TRANSFERASE Compound GLUTATHIONE S-TRANSFERASE P1-1 Source Homo sapiens (Human) (GTP_HUMAN) Sequence B:  PYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEG SLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGK DQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA LPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLI HEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNL PINGNGKQ Description Functional site 1) chain B residue 66 type sequence N description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 2) chain B residue 70 type sequence R description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 3) chain B residue 94 type sequence D description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 4) chain B residue 97 type sequence E description BINDING SITE FOR RESIDUE SO4 A 210 source : AC1 5) chain B residue 98 type sequence D description BINDING SITE FOR RESIDUE GSH A 211 source : AC2 6) chain B residue 171 type sequence D description BINDING SITE FOR RESIDUE MES A 213 source : AC4 7) chain B residue 8 type sequence F description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 8) chain B residue 13 type sequence R description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 9) chain B residue 38 type sequence W description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 10) chain B residue 44 type sequence K description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 11) chain B residue 51 type sequence Q description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 12) chain B residue 52 type sequence L description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 13) chain B residue 53 type sequence P description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 14) chain B residue 64 type sequence Q description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 15) chain B residue 65 type sequence S description BINDING SITE FOR RESIDUE GSH B 210 source : AC5 16) chain B residue 7 type sequence Y description BINDING SITE FOR RESIDUE EAA B 211 source : AC6 17) chain B residue 8 type sequence F description BINDING SITE FOR RESIDUE EAA B 211 source : AC6 18) chain B residue 10 type sequence V description BINDING SITE FOR RESIDUE EAA B 211 source : AC6 19) chain B residue 104 type sequence I description BINDING SITE FOR RESIDUE EAA B 211 source : AC6 20) chain B residue 108 type sequence Y description BINDING SITE FOR RESIDUE EAA B 211 source : AC6 21) chain B residue 22 type sequence A description BINDING SITE FOR RESIDUE MES B 212 source : AC7 22) chain B residue 28 type sequence W description BINDING SITE FOR RESIDUE MES B 212 source : AC7 23) chain B residue 30 type sequence E description BINDING SITE FOR RESIDUE MES B 212 source : AC7 24) chain B residue 197 type sequence E description BINDING SITE FOR RESIDUE MES B 212 source : AC7 25) chain B residue 45 type BINDING sequence A 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 26) chain B residue 52 type BINDING sequence L 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 65 type BINDING sequence S 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 8 type BINDING sequence F 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 14 type BINDING sequence C 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 39 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 31) chain B residue 4 type MOD_RES sequence T description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 199 type MOD_RES sequence V description Phosphotyrosine; by EGFR => ECO:0000269|PubMed:19254954 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 62 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 103 type MOD_RES sequence Y description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 116 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P19157 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 128 type MOD_RES sequence P description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links