eF-site ID 1dlg-AB
PDB Code 1dlg
Chain A, B

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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
B:  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 B
residue 252
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 1501
source : AC2

7) chain B
residue 253
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 1501
source : AC2

8) chain A
residue 401
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 1502
source : AC3

9) chain A
residue 403
type
sequence E
description BINDING SITE FOR RESIDUE PO4 A 1502
source : AC3

10) chain A
residue 404
type
sequence D
description BINDING SITE FOR RESIDUE PO4 A 1502
source : AC3

11) chain A
residue 407
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 1502
source : AC3

12) chain A
residue 415
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 1502
source : AC3

13) chain A
residue 162
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 1503
source : AC4

14) chain A
residue 163
type
sequence V
description BINDING SITE FOR RESIDUE PO4 A 1503
source : AC4

15) chain A
residue 164
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 1503
source : AC4

16) chain B
residue 23
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 1504
source : AC5

17) chain B
residue 305
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 1504
source : AC5

18) chain B
residue 371
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 1504
source : AC5

19) chain A
residue 118
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 1506
source : AC6

20) chain A
residue 119
type
sequence A
description BINDING SITE FOR RESIDUE PO4 B 1506
source : AC6

21) chain B
residue 119
type
sequence A
description BINDING SITE FOR RESIDUE PO4 B 1506
source : AC6

22) chain B
residue 159
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 1506
source : AC6

23) chain B
residue 160
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 1506
source : AC6

24) chain B
residue 92
type
sequence A
description BINDING SITE FOR RESIDUE PO4 B 1507
source : AC7

25) chain B
residue 95
type
sequence W
description BINDING SITE FOR RESIDUE PO4 B 1507
source : AC7

26) chain B
residue 319
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 1508
source : AC8

27) chain B
residue 320
type
sequence T
description BINDING SITE FOR RESIDUE PO4 B 1508
source : AC8

28) chain B
residue 355
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 1508
source : AC8

29) chain B
residue 393
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 B 1509
source : AC9

30) chain B
residue 394
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 1509
source : AC9

31) chain B
residue 397
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 1509
source : AC9

32) chain A
residue 250
type
sequence V
description BINDING SITE FOR RESIDUE HAI B 1420
source : BC1

33) chain A
residue 279
type
sequence W
description BINDING SITE FOR RESIDUE HAI B 1420
source : BC1

34) chain B
residue 279
type
sequence W
description BINDING SITE FOR RESIDUE HAI B 1420
source : BC1

35) chain A
residue 250
type
sequence V
description BINDING SITE FOR RESIDUE HAI B 1422
source : BC2

36) chain A
residue 274
type
sequence E
description BINDING SITE FOR RESIDUE HAI B 1422
source : BC2

37) chain A
residue 281
type
sequence S
description BINDING SITE FOR RESIDUE HAI B 1422
source : BC2

38) chain B
residue 250
type
sequence V
description BINDING SITE FOR RESIDUE HAI B 1422
source : BC2

39) chain B
residue 274
type
sequence E
description BINDING SITE FOR RESIDUE HAI B 1422
source : BC2

40) chain B
residue 281
type
sequence S
description BINDING SITE FOR RESIDUE HAI B 1422
source : BC2

41) chain A
residue 80
type
sequence F
description BINDING SITE FOR RESIDUE HAI A 1424
source : BC3

42) chain A
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE HAI A 1424
source : BC3

43) chain A
residue 144
type
sequence K
description BINDING SITE FOR RESIDUE HAI A 1424
source : BC3

44) chain A
residue 148
type
sequence N
description BINDING SITE FOR RESIDUE HAI A 1424
source : BC3

45) chain A
residue 22
type catalytic
sequence K
description 369
source MCSA : MCSA1

46) chain A
residue 23
type catalytic
sequence N
description 369
source MCSA : MCSA1

47) chain A
residue 115
type catalytic
sequence S
description 369
source MCSA : MCSA1

48) chain A
residue 120
type catalytic
sequence R
description 369
source MCSA : MCSA1

49) chain A
residue 305
type catalytic
sequence D
description 369
source MCSA : MCSA1

50) chain A
residue 397
type catalytic
sequence R
description 369
source MCSA : MCSA1

51) chain B
residue 22
type catalytic
sequence K
description 369
source MCSA : MCSA2

52) chain B
residue 23
type catalytic
sequence N
description 369
source MCSA : MCSA2

53) chain B
residue 115
type catalytic
sequence S
description 369
source MCSA : MCSA2

54) chain B
residue 120
type catalytic
sequence R
description 369
source MCSA : MCSA2

55) chain B
residue 305
type catalytic
sequence D
description 369
source MCSA : MCSA2

56) chain B
residue 397
type catalytic
sequence R
description 369
source MCSA : MCSA2

57) 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

58) chain B
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

59) chain A
residue 22
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ
source Swiss-Prot : SWS_FT_FI2

60) chain B
residue 22
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ
source Swiss-Prot : SWS_FT_FI2

61) chain A
residue 91
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI3

62) chain B
residue 91
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00111
source Swiss-Prot : SWS_FT_FI3

63) 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

64) 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

65) 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

66) 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

67) 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

68) 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

69) chain A
residue 160
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ
source Swiss-Prot : SWS_FT_FI5

70) chain B
residue 160
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ
source Swiss-Prot : SWS_FT_FI5

71) 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

72) chain B
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


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