eF-site ID 5n6h-A PDB Code 5n6h Chain A click to enlarge Title Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli Classification MEMBRANE PROTEIN Compound Apolipoprotein N-acyltransferase Source (LNT_ECOLI) Sequence A:  LIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQ ALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATFGGM PGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWLRVA IAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAP IMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLFALP FPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNT LKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALD GELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPY SYESADRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSF SRGPYIQPPLSANGIELTAAICYEIILGEQVRDNFRPDTD YLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLRSTN NGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYAR TGNWPLWVLTALFGFAAVLMSLR Description (1)  Apolipoprotein N-acyltransferase (E.C.2.3.1.-) Functional site 1) chain A residue 22 type sequence A description binding site for residue OLC A 601 source : AC1 2) chain A residue 25 type sequence T description binding site for residue OLC A 601 source : AC1 3) chain A residue 26 type sequence L description binding site for residue OLC A 601 source : AC1 4) chain A residue 31 type sequence Y description binding site for residue OLC A 601 source : AC1 5) chain A residue 70 type sequence S description binding site for residue OLC A 601 source : AC1 6) chain A residue 73 type sequence N description binding site for residue OLC A 601 source : AC1 7) chain A residue 13 type sequence R description binding site for residue OLC A 602 source : AC2 8) chain A residue 46 type sequence A description binding site for residue OLC A 602 source : AC2 9) chain A residue 47 type sequence L description binding site for residue OLC A 602 source : AC2 10) chain A residue 49 type sequence F description binding site for residue OLC A 602 source : AC2 11) chain A residue 50 type sequence N description binding site for residue OLC A 602 source : AC2 12) chain A residue 188 type sequence V description binding site for residue OLC A 602 source : AC2 13) chain A residue 121 type sequence W description binding site for residue OLC A 603 source : AC3 14) chain A residue 171 type sequence A description binding site for residue OLC A 603 source : AC3 15) chain A residue 178 type sequence M description binding site for residue OLC A 603 source : AC3 16) chain A residue 191 type sequence N description binding site for residue OLC A 603 source : AC3 17) chain A residue 197 type sequence V description binding site for residue OLC A 603 source : AC3 18) chain A residue 10 type sequence Q description binding site for residue OLC A 604 source : AC4 19) chain A residue 52 type sequence R description binding site for residue OLC A 604 source : AC4 20) chain A residue 55 type sequence Q description binding site for residue OLC A 604 source : AC4 21) chain A residue 58 type sequence A description binding site for residue OLC A 604 source : AC4 22) chain A residue 61 type sequence F description binding site for residue OLC A 604 source : AC4 23) chain A residue 131 type sequence L description binding site for residue OLC A 605 source : AC5 24) chain A residue 134 type sequence V description binding site for residue OLC A 605 source : AC5 25) chain A residue 488 type sequence N description binding site for residue OLC A 605 source : AC5 26) chain A residue 489 type sequence W description binding site for residue OLC A 605 source : AC5 27) chain A residue 492 type sequence W description binding site for residue OLC A 605 source : AC5 28) chain A residue 499 type sequence G description binding site for residue OLC A 605 source : AC5 29) chain A residue 52 type sequence R description binding site for residue OLC A 606 source : AC6 30) chain A residue 54 type sequence L description binding site for residue OLC A 606 source : AC6 31) chain A residue 107 type sequence L description binding site for residue OLC A 606 source : AC6 32) chain A residue 114 type sequence R description binding site for residue OLC A 606 source : AC6 33) chain A residue 18 type sequence L description binding site for residue OLC A 607 source : AC7 34) chain A residue 62 type sequence C description binding site for residue OLC A 607 source : AC7 35) chain A residue 134 type sequence V description binding site for residue OLC A 608 source : AC8 36) chain A residue 137 type sequence F description binding site for residue OLC A 608 source : AC8 37) chain A residue 170 type sequence E description binding site for residue OLC A 608 source : AC8 38) chain A residue 488 type sequence N description binding site for residue OLC A 608 source : AC8 39) chain A residue 492 type sequence W description binding site for residue OLC A 608 source : AC8 40) chain A residue 485 type sequence R description binding site for residue OLC A 609 source : AC9 41) chain A residue 341 type sequence F description binding site for residue OLC A 610 source : AD1 42) chain A residue 22 type sequence A description binding site for residue OLC A 611 source : AD2 43) chain A residue 69 type sequence G description binding site for residue OLC A 611 source : AD2 44) chain A residue 73 type sequence N description binding site for residue OLC A 611 source : AD2 45) chain A residue 76 type sequence Y description binding site for residue OLC A 611 source : AD2 46) chain A residue 94 type sequence V description binding site for residue OLC A 611 source : AD2 47) chain A residue 95 type sequence V description binding site for residue OLC A 611 source : AD2 48) chain A residue 190 type sequence R description binding site for residue OLC A 612 source : AD3 49) chain A residue 192 type sequence W description binding site for residue OLC A 612 source : AD3 50) chain A residue 143 type sequence L description binding site for residue GOL A 613 source : AD4 51) chain A residue 141 type sequence W description binding site for residue GOL A 614 source : AD5 52) chain A residue 203 type sequence A description binding site for residue GOL A 615 source : AD6 53) chain A residue 206 type sequence F description binding site for residue GOL A 615 source : AD6 54) chain A residue 239 type sequence E description binding site for residue GOL A 616 source : AD7 55) chain A residue 243 type sequence L description binding site for residue GOL A 616 source : AD7 56) chain A residue 277 type sequence Q description binding site for residue GOL A 616 source : AD7 57) chain A residue 279 type sequence P description binding site for residue GOL A 616 source : AD7 58) chain A residue 280 type sequence F description binding site for residue GOL A 616 source : AD7 59) chain A residue 10 type sequence Q description binding site for residue GOL A 617 source : AD8 60) chain A residue 11 type sequence R description binding site for residue GOL A 617 source : AD8 61) chain A residue 258 type sequence G description binding site for residue GOL A 618 source : AD9 62) chain A residue 259 type sequence K description binding site for residue GOL A 618 source : AD9 63) chain A residue 261 type sequence S description binding site for residue GOL A 618 source : AD9 64) chain A residue 291 type sequence K description binding site for residue GOL A 618 source : AD9 65) chain A residue 292 type sequence G description binding site for residue GOL A 618 source : AD9 66) chain A residue 293 type sequence S description binding site for residue GOL A 618 source : AD9 67) chain A residue 86 type sequence P description binding site for residue OLC B 602 source : AE2 68) chain A residue 88 type sequence P description binding site for residue OLC B 602 source : AE2 69) chain A residue 89 type sequence V description binding site for residue OLC B 602 source : AE2 70) chain A residue 54 type sequence L description binding site for residue OLC B 605 source : AE5 71) chain A residue 49-52 type TOPO_DOM sequence FNRR description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 117-120 type TOPO_DOM sequence PKTT description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 190-191 type TOPO_DOM sequence RN description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 10-27 type TRANSMEM sequence QRIRLLLALLFGACGTLA description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 75) chain A residue 34-48 type TRANSMEM sequence WPAAIISLMGLQALT description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 53-68 type TRANSMEM sequence PLQSAAIGFCWGFGLF description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 77) chain A residue 87-116 type TRANSMEM sequence GPVNIFLVVLLAAYLSLYTGLFAGVLSRLW description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 78) chain A residue 121-141 type TRANSMEM sequence WLRVAIAAPALWQVTEFLRGW description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 79) chain A residue 169-189 type TRANSMEM sequence VEAINFLLMMVSGLLALALVK description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 80) chain A residue 192-210 type TRANSMEM sequence WRPLVVAVVLFALPFPLRY description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 81) chain A residue 488-508 type TRANSMEM sequence NWPLWVLTALFGFAAVLMSLR description Helical => ECO:0000269|PubMed:28675161 source Swiss-Prot : SWS_FT_FI2 82) chain A residue 28-33 type TOPO_DOM sequence FSPYDV description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 69-86 type TOPO_DOM sequence GSGINWVYVSIATFGGMP description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI3 84) chain A residue 142-168 type TOPO_DOM sequence VLTGFPWLQFGYSQIDGPLKGLAPIMG description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 211-487 type TOPO_DOM sequence IQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYY NATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRD KGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESA DRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSFSRGPY IQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTI SNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITA VIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTG description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614 source Swiss-Prot : SWS_FT_FI3 86) chain A residue 267 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161 source Swiss-Prot : SWS_FT_FI4 87) chain A residue 335 type ACT_SITE sequence K description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161 source Swiss-Prot : SWS_FT_FI5 88) chain A residue 387 type ACT_SITE sequence C description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161 source Swiss-Prot : SWS_FT_FI6

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