eF-site ID 3kqa-A PDB Code 3kqa Chain A click to enlarge Title MurA dead-end complex with terreic acid Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase Source Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56) (MURA_ENTCL) Sequence A:  MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVE IQNVPKLKDIDTTMKLLTQLGTKVERXGSVWIDASNVNNF SAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGAR PVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDK VSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVA LGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLV AAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWI SLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGT GVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKL SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE RIEDKLRALGANIERVKGE Description Functional site 1) chain A residue 115 type sequence C description BINDING SITE FOR RESIDUE TR9 A 500 source : AC1 2) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE TR9 A 500 source : AC1 3) chain A residue 138 type sequence L description BINDING SITE FOR RESIDUE TR9 A 500 source : AC1 4) chain A residue 130 type sequence E description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 5) chain A residue 138 type sequence L description BINDING SITE FOR RESIDUE CA A 420 source : AC5 6) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE CA A 421 source : AC6 7) chain A residue 136 type sequence I description BINDING SITE FOR RESIDUE CA B 420 source : AC7 8) chain A residue 22 type catalytic sequence K description 369 source MCSA : MCSA1 9) chain A residue 23 type catalytic sequence N description 369 source MCSA : MCSA1 10) chain A residue 115 type catalytic sequence C description 369 source MCSA : MCSA1 11) chain A residue 120 type catalytic sequence R description 369 source MCSA : MCSA1 12) chain A residue 305 type catalytic sequence D description 369 source MCSA : MCSA1 13) chain A residue 397 type catalytic sequence R description 369 source MCSA : MCSA1 14) chain A residue 115 type ACT_SITE sequence C description Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH source Swiss-Prot : SWS_FT_FI1 15) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 16) chain A residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 17) 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 18) 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 19) 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 20) chain A residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 21) chain A residue 115 type MOD_RES sequence C description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 source Swiss-Prot : SWS_FT_FI6

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