eF-site ID 5h5l-AB PDB Code 5h5l Chain A, B click to enlarge Title Structure of prostaglandin synthase D of Nilaparvata lugens Classification TRANSFERASE Compound Glutathione s-transferase S2 Source Nilaparvata lugens (Brown planthopper) (J9Q529_NILLU) Sequence A:  PTYKLTYFNFAGLGEPIRWMLSYLDVPFEDNRIEREQWPT IKSTTPYGQVPVLEVDGKQVCQSTAIARYLGKKAGLAGSN EWEDLMIDTMIDTFNDFRSSISKWFRDEATKKKLEETLLN ETVPFYFNKFNDHIKNNGGYLANGKLSWGDIYFISILEFM TTIWSDIIDKYEHIKALNDKVVNLPKIKAWIEKRPV B:  PTYKLTYFNFAGLGEPIRWMLSYLDVPFEDNRIEREQWPT IKSTTPYGQVPVLEVDGKQVCQSTAIARYLGKKAGLAGSN EWEDLMIDTMIDTFNDFRSSISKWFRESDEATKKKLEETL LNETVPFYFNKFNDHIKNNGGYLANGKLSWGDIYFISILE FMTTIWSDIIDKYEHIKALNDKVVNLPKIKAWIEKRPVP Description Functional site 1) chain A residue 8 type sequence Y description binding site for residue GSH A 301 source : AC1 2) chain A residue 14 type sequence L description binding site for residue GSH A 301 source : AC1 3) chain A residue 39 type sequence W description binding site for residue GSH A 301 source : AC1 4) chain A residue 43 type sequence K description binding site for residue GSH A 301 source : AC1 5) chain A residue 50 type sequence Q description binding site for residue GSH A 301 source : AC1 6) chain A residue 51 type sequence V description binding site for residue GSH A 301 source : AC1 7) chain A residue 52 type sequence P description binding site for residue GSH A 301 source : AC1 8) chain A residue 63 type sequence Q description binding site for residue GSH A 301 source : AC1 9) chain A residue 64 type sequence S description binding site for residue GSH A 301 source : AC1 10) chain B residue 97 type sequence D description binding site for residue GSH A 301 source : AC1 11) chain A residue 8 type sequence Y description binding site for residue PEG A 302 source : AC2 12) chain A residue 13 type sequence G description binding site for residue PEG A 302 source : AC2 13) chain A residue 99 type sequence R description binding site for residue PEG A 302 source : AC2 14) chain A residue 102 type sequence I description binding site for residue PEG A 302 source : AC2 15) chain A residue 103 type sequence S description binding site for residue PEG A 302 source : AC2 16) chain A residue 97 type sequence D description binding site for residue GSH B 301 source : AC3 17) chain B residue 8 type sequence Y description binding site for residue GSH B 301 source : AC3 18) chain B residue 14 type sequence L description binding site for residue GSH B 301 source : AC3 19) chain B residue 39 type sequence W description binding site for residue GSH B 301 source : AC3 20) chain B residue 43 type sequence K description binding site for residue GSH B 301 source : AC3 21) chain B residue 50 type sequence Q description binding site for residue GSH B 301 source : AC3 22) chain B residue 51 type sequence V description binding site for residue GSH B 301 source : AC3 23) chain B residue 52 type sequence P description binding site for residue GSH B 301 source : AC3 24) chain B residue 63 type sequence Q description binding site for residue GSH B 301 source : AC3 25) chain B residue 64 type sequence S description binding site for residue GSH B 301 source : AC3 26) chain B residue 134 type sequence N description binding site for residue EDO B 303 source : AC5 27) chain B residue 135 type sequence D description binding site for residue EDO B 303 source : AC5 28) chain B residue 138 type sequence K description binding site for residue EDO B 303 source : AC5 29) chain B residue 176 type sequence H description binding site for residue EDO B 303 source : AC5 30) chain A residue 25 type sequence L description binding site for residue EDO B 304 source : AC6 31) chain A residue 74 type sequence K description binding site for residue EDO B 304 source : AC6 32) chain A residue 75 type sequence A description binding site for residue EDO B 304 source : AC6 33) chain B residue 131 type sequence N description binding site for residue EDO B 304 source : AC6 34) chain B residue 174 type sequence Y description binding site for residue EDO B 304 source : AC6

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