eF-site ID 3kqa-ABCD PDB Code 3kqa Chain A, B, C, D 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 B:  MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVE IQNVPKLKDIDTTMKLLTQLGTKVERXGSVWIDASNVNNF SAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGAR PVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDK VSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVA LGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLV AAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWI SLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGT GVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKL SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE RIEDKLRALGANIERVKGE C:  MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVE IQNVPKLKDIDTTMKLLTQLGTKVERXGSVWIDASNVNNF SAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGAR PVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDK VSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVA LGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLV AAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWI SLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGT GVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKL SGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE RIEDKLRALGANIERVKGE D:  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 B residue 130 type sequence E description BINDING SITE FOR RESIDUE TR9 A 500 source : AC1 5) chain A residue 130 type sequence E description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 6) chain B residue 115 type sequence C description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 7) chain B residue 116 type sequence A description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 8) chain B residue 137 type sequence K description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 9) chain B residue 138 type sequence L description BINDING SITE FOR RESIDUE TR9 B 500 source : AC2 10) chain C residue 115 type sequence C description BINDING SITE FOR RESIDUE TR9 C 500 source : AC3 11) chain C residue 116 type sequence A description BINDING SITE FOR RESIDUE TR9 C 500 source : AC3 12) chain C residue 138 type sequence L description BINDING SITE FOR RESIDUE TR9 C 500 source : AC3 13) chain D residue 127 type sequence F description BINDING SITE FOR RESIDUE TR9 C 500 source : AC3 14) chain D residue 130 type sequence E description BINDING SITE FOR RESIDUE TR9 C 500 source : AC3 15) chain C residue 126 type sequence I description BINDING SITE FOR RESIDUE TR9 D 500 source : AC4 16) chain C residue 127 type sequence F description BINDING SITE FOR RESIDUE TR9 D 500 source : AC4 17) chain C residue 130 type sequence E description BINDING SITE FOR RESIDUE TR9 D 500 source : AC4 18) chain D residue 115 type sequence C description BINDING SITE FOR RESIDUE TR9 D 500 source : AC4 19) chain D residue 116 type sequence A description BINDING SITE FOR RESIDUE TR9 D 500 source : AC4 20) chain D residue 138 type sequence L description BINDING SITE FOR RESIDUE TR9 D 500 source : AC4 21) chain A residue 138 type sequence L description BINDING SITE FOR RESIDUE CA A 420 source : AC5 22) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE CA A 421 source : AC6 23) chain A residue 136 type sequence I description BINDING SITE FOR RESIDUE CA B 420 source : AC7 24) chain B residue 136 type sequence I description BINDING SITE FOR RESIDUE CA B 420 source : AC7 25) chain B residue 138 type sequence L description BINDING SITE FOR RESIDUE CA B 421 source : AC8 26) chain B residue 116 type sequence A description BINDING SITE FOR RESIDUE CA B 422 source : AC9 27) chain B residue 104 type sequence F description BINDING SITE FOR RESIDUE CA B 423 source : BC1 28) chain B residue 106 type sequence Q description BINDING SITE FOR RESIDUE CA B 423 source : BC1 29) chain C residue 148 type sequence N description BINDING SITE FOR RESIDUE CA B 423 source : BC1 30) chain C residue 116 type sequence A description BINDING SITE FOR RESIDUE CA C 420 source : BC2 31) chain C residue 138 type sequence L description BINDING SITE FOR RESIDUE CA C 421 source : BC3 32) chain D residue 130 type sequence E description BINDING SITE FOR RESIDUE CA C 421 source : BC3 33) chain C residue 130 type sequence E description BINDING SITE FOR RESIDUE CA D 420 source : BC4 34) chain D residue 138 type sequence L description BINDING SITE FOR RESIDUE CA D 420 source : BC4 35) chain D residue 116 type sequence A description BINDING SITE FOR RESIDUE CA D 421 source : BC5 36) chain A residue 22 type catalytic sequence K description 369 source MCSA : MCSA1 37) chain A residue 23 type catalytic sequence N description 369 source MCSA : MCSA1 38) chain A residue 115 type catalytic sequence C description 369 source MCSA : MCSA1 39) chain A residue 120 type catalytic sequence R description 369 source MCSA : MCSA1 40) chain A residue 305 type catalytic sequence D description 369 source MCSA : MCSA1 41) chain A residue 397 type catalytic sequence R description 369 source MCSA : MCSA1 42) chain B residue 22 type catalytic sequence K description 369 source MCSA : MCSA2 43) chain B residue 23 type catalytic sequence N description 369 source MCSA : MCSA2 44) chain B residue 115 type catalytic sequence C description 369 source MCSA : MCSA2 45) chain B residue 120 type catalytic sequence R description 369 source MCSA : MCSA2 46) chain B residue 305 type catalytic sequence D description 369 source MCSA : MCSA2 47) chain B residue 397 type catalytic sequence R description 369 source MCSA : MCSA2 48) chain C residue 22 type catalytic sequence K description 369 source MCSA : MCSA3 49) chain C residue 23 type catalytic sequence N description 369 source MCSA : MCSA3 50) chain C residue 115 type catalytic sequence C description 369 source MCSA : MCSA3 51) chain C residue 120 type catalytic sequence R description 369 source MCSA : MCSA3 52) chain C residue 305 type catalytic sequence D description 369 source MCSA : MCSA3 53) chain C residue 397 type catalytic sequence R description 369 source MCSA : MCSA3 54) chain D residue 22 type catalytic sequence K description 369 source MCSA : MCSA4 55) chain D residue 23 type catalytic sequence N description 369 source MCSA : MCSA4 56) chain D residue 115 type catalytic sequence C description 369 source MCSA : MCSA4 57) chain D residue 120 type catalytic sequence R description 369 source MCSA : MCSA4 58) chain D residue 305 type catalytic sequence D description 369 source MCSA : MCSA4 59) chain D residue 397 type catalytic sequence R description 369 source MCSA : MCSA4 60) 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 61) 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 62) chain C 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 63) chain D 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 64) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 65) chain B residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 66) chain C residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 67) chain D residue 22 type BINDING sequence K description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI2 68) chain A residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 69) chain B residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 70) chain C residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 71) chain D residue 91 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 72) 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 73) chain D 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 74) chain D 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 75) chain D 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 76) 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 77) 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 78) 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 79) 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 80) 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 81) chain C 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 82) chain C 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 83) chain C 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 84) chain A residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 85) chain B residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 86) chain C residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 87) chain D residue 160 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ source Swiss-Prot : SWS_FT_FI5 88) 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 89) 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 90) chain C 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 91) chain D 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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