eF-site ID 5xj8-AB PDB Code 5xj8 Chain A, B click to enlarge Title Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the lysphosphatidic acid form Classification TRANSFERASE Compound Glycerol-3-phosphate acyltransferase Source Aquifex aeolicus (strain VF5) (PLSY_AQUAE) Sequence A:  GSALFLVIFAYLLGSITFGEVIAKLKGVDGSGNVGATNVT RALGKKYGVLVFFLDFLKGFIPALIAVKSFGIDSWVLTFT GLASVLGHMYPVFFGFKGGKGVATALGVVFAVSPSVALFS FLVWLGIFLWKRYVSLASITATISAFLFLFVAGYPVNVLF MAIVIGALIIYRHRENINRLLTGREHRFGTLEVLFQ B:  GSALFLVIFAYLLGSITFGEVIAKLKGVDLRNVGSGNVGA TNVTRALGKKYGVLVFFLDFLKGFIPALIAVKSFGIDSWV LTFTGLASVLGHMYPVFFGFKGGKGVATALGVVFAVSPSV ALFSFLVWLGIFLWKRYVSLASITATISAFLFLFVAGYPV NVLFMAIVIGALIIYRHRENINRLLTGREHRFGTLEVLF Description Functional site 1) chain A residue 26 type sequence K description binding site for residue PO4 A 301 source : AC1 2) chain A residue 135 type sequence K description binding site for residue PO4 A 301 source : AC1 3) chain A residue 191 type sequence R description binding site for residue PO4 A 301 source : AC1 4) chain A residue 92 type sequence H description binding site for residue PO4 A 302 source : AC2 5) chain A residue 104 type sequence K description binding site for residue PO4 A 302 source : AC2 6) chain A residue 105 type sequence G description binding site for residue PO4 A 302 source : AC2 7) chain A residue 106 type sequence V description binding site for residue PO4 A 302 source : AC2 8) chain A residue 107 type sequence A description binding site for residue PO4 A 302 source : AC2 9) chain B residue 37 type sequence N description binding site for residue PO4 B 301 source : AC3 10) chain B residue 39 type sequence G description binding site for residue PO4 B 301 source : AC3 11) chain B residue 92 type sequence H description binding site for residue PO4 B 301 source : AC3 12) chain B residue 103 type sequence G description binding site for residue PO4 B 301 source : AC3 13) chain B residue 104 type sequence K description binding site for residue PO4 B 301 source : AC3 14) chain B residue 105 type sequence G description binding site for residue PO4 B 301 source : AC3 15) chain B residue 106 type sequence V description binding site for residue PO4 B 301 source : AC3 16) chain B residue 35 type sequence S description binding site for residue NKO B 302 source : AC4 17) chain B residue 37 type sequence N description binding site for residue NKO B 302 source : AC4 18) chain B residue 40 type sequence A description binding site for residue NKO B 302 source : AC4 19) chain B residue 41 type sequence T description binding site for residue NKO B 302 source : AC4 20) chain B residue 42 type sequence N description binding site for residue NKO B 302 source : AC4 21) chain B residue 45 type sequence R description binding site for residue NKO B 302 source : AC4 22) chain B residue 56 type sequence F description binding site for residue NKO B 302 source : AC4 23) chain B residue 104 type sequence K description binding site for residue NKO B 302 source : AC4 24) chain B residue 106 type sequence V description binding site for residue NKO B 302 source : AC4 25) chain B residue 110 type sequence L description binding site for residue NKO B 302 source : AC4 26) chain B residue 113 type sequence V description binding site for residue NKO B 302 source : AC4 27) chain B residue 125 type sequence F description binding site for residue NKO B 302 source : AC4 28) chain B residue 128 type sequence W description binding site for residue NKO B 302 source : AC4 29) chain B residue 142 type sequence S description binding site for residue NKO B 302 source : AC4 30) chain B residue 177 type sequence H description binding site for residue NKO B 302 source : AC4 31) chain B residue 180 type sequence N description binding site for residue NKO B 302 source : AC4 32) chain A residue 3-23 type TRANSMEM sequence ALFLVIFAYLLGSITFGEVIA description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 149-169 type TRANSMEM sequence AFLFLFVAGYPVNVLFMAIVI description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 51-71 type TRANSMEM sequence YGVLVFFLDFLKGFIPALIAV description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 80-100 type TRANSMEM sequence VLTFTGLASVLGHMYPVFFGF description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 112-132 type TRANSMEM sequence VVFAVSPSVALFSFLVWLGIF description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 149-169 type TRANSMEM sequence AFLFLFVAGYPVNVLFMAIVI description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 3-23 type TRANSMEM sequence ALFLVIFAYLLGSITFGEVIA description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 51-71 type TRANSMEM sequence YGVLVFFLDFLKGFIPALIAV description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 80-100 type TRANSMEM sequence VLTFTGLASVLGHMYPVFFGF description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 112-132 type TRANSMEM sequence VVFAVSPSVALFSFLVWLGIF description Helical => ECO:0000255|HAMAP-Rule:MF_01043 source Swiss-Prot : SWS_FT_FI1

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