eF-site ID 3kqj-A PDB Code 3kqj Chain A click to enlarge Title MurA binary complex with UDP-N-acetylglucosamine Classification TRANSFERASE Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase Source null (MURA_ECOLI) Sequence A:  MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVE IQNVPKLKDVDTSMKLLSQLGAKVERXGSVHIDARDVNVF CAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGAR PVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDK VSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLIT LGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLV AAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWI SLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGT GFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKL SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE RIEDKLRALGANIERVKGE Description Functional site 1) chain A residue 155 type sequence H description BINDING SITE FOR RESIDUE GOL A 420 source : AC1 2) chain A residue 322 type sequence F description BINDING SITE FOR RESIDUE GOL A 420 source : AC1 3) chain A residue 351 type sequence T description BINDING SITE FOR RESIDUE GOL A 420 source : AC1 4) chain A residue 22 type sequence K description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 5) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 6) chain A residue 91 type sequence R description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 7) chain A residue 95 type sequence W description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 8) chain A residue 120 type sequence R description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 9) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 10) chain A residue 122 type sequence V description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 11) chain A residue 123 type sequence D description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 12) chain A residue 124 type sequence L description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 13) chain A residue 125 type sequence H description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 14) chain A residue 160 type sequence K description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 15) chain A residue 162 type sequence S description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 16) chain A residue 163 type sequence V description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 17) chain A residue 164 type sequence G description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 18) chain A residue 304 type sequence T description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 19) chain A residue 305 type sequence D description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 20) chain A residue 327 type sequence V description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 21) chain A residue 328 type sequence F description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 22) chain A residue 331 type sequence R description BINDING SITE FOR RESIDUE UD1 A 450 source : AC2 23) chain A residue 22 type sequence K description BINDING SITE FOR RESIDUE PO4 A 421 source : AC3 24) chain A residue 114 type sequence G description BINDING SITE FOR RESIDUE PO4 A 421 source : AC3 25) chain A residue 115 type sequence C description BINDING SITE FOR RESIDUE PO4 A 421 source : AC3 26) chain A residue 120 type sequence R description BINDING SITE FOR RESIDUE PO4 A 421 source : AC3 27) chain A residue 397 type sequence R description BINDING SITE FOR RESIDUE PO4 A 421 source : AC3 28) chain A residue 115 type MOD_RES sequence C description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000305|PubMed:22378791 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 115 type ACT_SITE sequence C description Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:8994972, ECO:0000305|PubMed:22378791, ECO:0007744|PDB:1UAE, ECO:0007744|PDB:3KR6 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:20392080, ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3KR6, ECO:0007744|PDB:3SWD source Swiss-Prot : SWS_FT_FI2 31) chain A residue 91 type BINDING sequence R description BINDING => ECO:0000269|PubMed:20392080, ECO:0007744|PDB:3KR6 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 327 type BINDING sequence V description BINDING => ECO:0000269|PubMed:20392080, ECO:0007744|PDB:3KR6 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6 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:3KR6 source Swiss-Prot : SWS_FT_FI4

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