eF-site ID 1dlg-A PDB Code 1dlg Chain A click to enlarge Title CRYSTAL STRUCTURE OF THE C115S ENTEROBACTER CLOACAE MURA IN THE UN-LIGANDED STATE Classification TRANSFERASE Compound UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE MURA Source Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56) (MURA_ENTCL) Sequence A:  MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVE IQNVPKLKDIDTTMKLLTQLGTKVERXGSVWIDASNVNNF SAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGSAIGAR PVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDK VSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVA LGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLV AAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWI SLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGT GVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKL SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE RIEDKLRALGANIERVKGE Description Functional site 1) chain A residue 135 type sequence E description BINDING SITE FOR RESIDUE PO4 A 1500 source : AC1 2) chain A residue 137 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1500 source : AC1 3) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE PO4 A 1500 source : AC1 4) chain A residue 252 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1501 source : AC2 5) chain A residue 278 type sequence D description BINDING SITE FOR RESIDUE PO4 B 1501 source : AC2 6) chain A residue 401 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1502 source : AC3 7) chain A residue 403 type sequence E description BINDING SITE FOR RESIDUE PO4 A 1502 source : AC3 8) chain A residue 404 type sequence D description BINDING SITE FOR RESIDUE PO4 A 1502 source : AC3 9) chain A residue 407 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1502 source : AC3 10) chain A residue 415 type sequence R description BINDING SITE FOR RESIDUE PO4 A 1502 source : AC3 11) chain A residue 162 type sequence S description BINDING SITE FOR RESIDUE PO4 A 1503 source : AC4 12) chain A residue 163 type sequence V description BINDING SITE FOR RESIDUE PO4 A 1503 source : AC4 13) chain A residue 164 type sequence G description BINDING SITE FOR RESIDUE PO4 A 1503 source : AC4 14) chain A residue 118 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1506 source : AC6 15) chain A residue 119 type sequence A description BINDING SITE FOR RESIDUE PO4 B 1506 source : AC6 16) chain A residue 250 type sequence V description BINDING SITE FOR RESIDUE HAI B 1420 source : BC1 17) chain A residue 279 type sequence W description BINDING SITE FOR RESIDUE HAI B 1420 source : BC1 18) chain A residue 250 type sequence V description BINDING SITE FOR RESIDUE HAI B 1422 source : BC2 19) chain A residue 274 type sequence E description BINDING SITE FOR RESIDUE HAI B 1422 source : BC2 20) chain A residue 281 type sequence S description BINDING SITE FOR RESIDUE HAI B 1422 source : BC2 21) chain A residue 80 type sequence F description BINDING SITE FOR RESIDUE HAI A 1424 source : BC3 22) chain A residue 135 type sequence E description BINDING SITE FOR RESIDUE HAI A 1424 source : BC3 23) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE HAI A 1424 source : BC3 24) chain A residue 148 type sequence N description BINDING SITE FOR RESIDUE HAI A 1424 source : BC3 25) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 26) chain A residue 115 type ACT_SITE sequence S description Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH source Swiss-Prot : SWS_FT_FI1 27) chain A residue 22 type catalytic sequence K description 369 source MCSA : MCSA1 28) chain A residue 23 type catalytic sequence N description 369 source MCSA : MCSA1 29) chain A residue 115 type catalytic sequence S description 369 source MCSA : MCSA1 30) chain A residue 120 type catalytic sequence R description 369 source MCSA : MCSA1 31) chain A residue 305 type catalytic sequence D description 369 source MCSA : MCSA1 32) chain A residue 397 type catalytic sequence R description 369 source MCSA : MCSA1 33) chain A residue 115 type MOD_RES sequence S description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI4 35) chain A residue 305 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI4 36) chain A residue 327 type BINDING sequence I description BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI4 37) chain A residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 38) chain A residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3

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