eF-site ID 3kqa-B PDB Code 3kqa Chain B click to enlarge Title MurA dead-end complex with terreic acid Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase Source null (MURA_ENTCL) Sequence B:  MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVE IQNVPKLKDIDTTMKLLTQLGTKVERXGSVWIDASNVNNF SAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGAR PVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDK VSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVA LGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLV AAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWI SLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGT GVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKL SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE RIEDKLRALGANIERVKGE Description Functional site 1) chain B residue 130 type sequence E description BINDING SITE FOR RESIDUE TR9 A 500 source : AC1 2) chain B residue 115 type sequence C description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 3) chain B residue 116 type sequence A description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 4) chain B residue 137 type sequence K description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 5) chain B residue 138 type sequence L description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 6) chain B residue 136 type sequence I description BINDING SITE FOR RESIDUE CA B 420 source : AC7 7) chain B residue 138 type sequence L description BINDING SITE FOR RESIDUE CA B 421 source : AC8 8) chain B residue 116 type sequence A description BINDING SITE FOR RESIDUE CA B 422 source : AC9 9) chain B residue 104 type sequence F description BINDING SITE FOR RESIDUE CA B 423 source : BC1 10) chain B residue 106 type sequence Q description BINDING SITE FOR RESIDUE CA B 423 source : BC1 11) chain B 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 12) chain B residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 13) chain B 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 14) chain B residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 15) chain B residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 16) chain B 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 17) chain B 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 18) chain B 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 19) chain B residue 22 type catalytic sequence K description 369 source MCSA : MCSA2 20) chain B residue 23 type catalytic sequence N description 369 source MCSA : MCSA2 21) chain B residue 115 type catalytic sequence C description 369 source MCSA : MCSA2 22) chain B residue 120 type catalytic sequence R description 369 source MCSA : MCSA2 23) chain B residue 305 type catalytic sequence D description 369 source MCSA : MCSA2 24) chain B residue 397 type catalytic sequence R description 369 source MCSA : MCSA2

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