eF-site ID 3swe-A PDB Code 3swe Chain A click to enlarge Title Haemophilus influenzae MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys117 Classification TRANSFERASE Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase Source Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (MURA_HAEIN) Sequence A:  MDKFRVYGQSRLSGSVNISGAKNAALPILFAAILATEPVK LTNVPELKDIETTLKILRQLGVVVDRDATGAVLLDASNIN HFTAPYELVKTMRASIWALAPLVARFHQGQVSLPGGXSIG ARPVDLHISGLEKLGADIVLEEGYVKAQVSDRLVGTRIVI EKVSVGATLSIMMAATLAKGTTVIENAAREPEIVDTADFL NKMGAKITGAGSAHITIEGVERLTGCEHSVVPDRIETGTF LIAAAISGGCVVCQNTKADTLDAVIDKLREAGAQVDVTEN SITLDMLGNRPKAVNIRTAPHPGFPTDMQAQFTLLNMVAE GTSIITETIFENRFMHIPELIRMGGKAEIEGNTAVCHGVE QLSGTEVIATDLRASISLVLAGCIATGETIVDRIYHIDRG YEHIEDKLRGLGAKIERFSG Description Functional site 1) chain A residue 278 type sequence T description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 2) chain A residue 279 type sequence E description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 3) chain A residue 280 type sequence N description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 4) chain A residue 281 type sequence S description BINDING SITE FOR RESIDUE SO4 A 501 source : AC1 5) chain A residue 157 type sequence R description BINDING SITE FOR RESIDUE SO4 A 502 source : AC2 6) chain A residue 269 type sequence R description BINDING SITE FOR RESIDUE SO4 A 502 source : AC2 7) chain A residue 81 type sequence H description BINDING SITE FOR RESIDUE SO4 A 503 source : AC3 8) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE SO4 A 503 source : AC3 9) chain A residue 83 type sequence T description BINDING SITE FOR RESIDUE SO4 A 503 source : AC3 10) chain A residue 208 type sequence T description BINDING SITE FOR RESIDUE SO4 A 504 source : AC4 11) chain A residue 209 type sequence G description BINDING SITE FOR RESIDUE SO4 A 504 source : AC4 12) chain A residue 210 type sequence A description BINDING SITE FOR RESIDUE SO4 A 504 source : AC4 13) chain A residue 55 type sequence K description BINDING SITE FOR RESIDUE SO4 A 505 source : AC5 14) chain A residue 58 type sequence R description BINDING SITE FOR RESIDUE SO4 A 505 source : AC5 15) chain A residue 395 type sequence Y description BINDING SITE FOR RESIDUE GOL A 506 source : AC6 16) chain A residue 396 type sequence H description BINDING SITE FOR RESIDUE GOL A 506 source : AC6 17) chain A residue 399 type sequence R description BINDING SITE FOR RESIDUE GOL A 506 source : AC6 18) chain A residue 152 type sequence R description BINDING SITE FOR RESIDUE GOL A 507 source : AC7 19) chain A residue 179 type sequence K description BINDING SITE FOR RESIDUE GOL A 507 source : AC7 20) chain A residue 219 type sequence G description BINDING SITE FOR RESIDUE GOL A 507 source : AC7 21) chain A residue 220 type sequence V description BINDING SITE FOR RESIDUE GOL A 507 source : AC7 22) chain A residue 221 type sequence E description BINDING SITE FOR RESIDUE GOL A 507 source : AC7 23) chain A residue 22 type sequence K description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 24) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 25) chain A residue 94 type sequence A description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 26) chain A residue 97 type sequence W description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 27) chain A residue 121 type sequence A description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 28) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 29) chain A residue 123 type sequence P description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 30) chain A residue 124 type sequence V description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 31) chain A residue 125 type sequence D description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 32) chain A residue 126 type sequence L description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 33) chain A residue 127 type sequence H description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 34) chain A residue 164 type sequence S description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 35) chain A residue 165 type sequence V description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 36) chain A residue 166 type sequence G description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 37) chain A residue 306 type sequence T description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 38) chain A residue 307 type sequence D description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 39) chain A residue 329 type sequence I description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 40) chain A residue 330 type sequence F description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 41) chain A residue 333 type sequence R description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 42) chain A residue 372 type sequence L description BINDING SITE FOR RESIDUE EPZ A 508 source : AC8 43) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI2 44) chain A residue 93 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 117 type ACT_SITE sequence X description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305|PubMed:22378791 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 117 type MOD_RES sequence X description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000305|PubMed:22378791 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 122 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4 48) chain A residue 164 type BINDING sequence S description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4 49) chain A residue 307 type BINDING sequence D description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWE source Swiss-Prot : SWS_FT_FI4 50) 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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