eF-site ID 2rl2-A PDB Code 2rl2 Chain A click to enlarge Title Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin Classification TRANSFERASE Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase Source Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (MURA_HAEIN) Sequence A:  MDKFRVYGQSRLSGSVNISGAKNAALPILFAAILATEPVK LTNVPELKDIETTLKILRQLGVVVDRDATGAVLLDASNIN HFTAPYELVKTMRASIWALAPLVARFHQGQVSLPGGCSIG ARPVDLHISGLEKLGADIVLEEGYVKAQVSDRLVGTRIVI EKVSVGATLSIMMAATLAKGTTVIENAAREPEIVDTADFL NKMGAKITGAGSAHITIEGVERLTGCEHSVVPDRIETGTF LIAAAISGGCVVCQNTKADTLDAVIDKLREAGAQVDVTEN SITLDMLGNRPKAVNIRTAPHPGFPTDMQAQFTLLNMVAE GTSIITETIFENRFMHIPELIRMGGKAEIEGNTAVCHGVE QLSGTEVIATDLRASISLVLAGCIATGETIVDRIYHIDRG YEHIEDKLRGLGAKIERFSG Description (1)  UDP-N-acetylglucosamine 1-carboxyvinyltransferase (E.C.2.5.1.7) Functional site 1) chain A residue 22 type sequence K description BINDING SITE FOR RESIDUE SO4 A 713 source : AC1 2) chain A residue 93 type sequence R description BINDING SITE FOR RESIDUE SO4 A 713 source : AC1 3) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE SO4 A 713 source : AC1 4) chain A residue 399 type sequence R description BINDING SITE FOR RESIDUE SO4 A 713 source : AC1 5) chain A residue 110 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 714 source : AC2 6) chain A residue 142 type sequence E description BINDING SITE FOR RESIDUE SO4 A 714 source : AC2 7) chain A residue 144 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 714 source : AC2 8) chain A residue 146 type sequence K description BINDING SITE FOR RESIDUE SO4 A 714 source : AC2 9) chain A residue 157 type sequence R description BINDING SITE FOR RESIDUE SO4 A 715 source : AC3 10) chain A residue 269 type sequence R description BINDING SITE FOR RESIDUE SO4 A 715 source : AC3 11) chain A residue 117 type sequence C description BINDING SITE FOR RESIDUE GG6 A 425 source : AC4 12) chain A residue 118 type sequence S description BINDING SITE FOR RESIDUE GG6 A 425 source : AC4 13) chain A residue 119 type sequence I description BINDING SITE FOR RESIDUE GG6 A 425 source : AC4 14) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 15) chain A residue 93 type sequence R description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 16) chain A residue 97 type sequence W description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 17) chain A residue 121 type sequence A description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 18) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 19) chain A residue 123 type sequence P description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 20) chain A residue 125 type sequence D description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 21) chain A residue 126 type sequence L description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 22) chain A residue 127 type sequence H description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 23) chain A residue 162 type sequence K description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 24) chain A residue 164 type sequence S description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 25) chain A residue 166 type sequence G description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 26) chain A residue 306 type sequence T description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 27) chain A residue 307 type sequence D description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 28) chain A residue 329 type sequence I description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 29) chain A residue 330 type sequence F description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 30) chain A residue 333 type sequence R description BINDING SITE FOR RESIDUE UD1 A 712 source : AC5 31) chain A residue 117 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305|PubMed:22378791 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI2 33) chain A residue 93 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 117 type MOD_RES sequence C description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305|PubMed:22378791 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 122 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4 36) chain A residue 164 type BINDING sequence S description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4 37) chain A residue 307 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4 38) chain A residue 329 type BINDING sequence I description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4

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