eF-site ID 3fk0-A
PDB Code 3fk0
Chain A

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Title E. coli EPSP synthase (TIPS mutation) liganded with S3P
Classification TRANSFERASE
Compound 3-phosphoshikimate 1-carboxyvinyltransferase
Source Escherichia coli (strain K12) (AROA_ECOLI)
Sequence A:  MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTV
LTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGG
PLHAEGALELFLGNAGIAMRSLAAALCLGSNDIVLTGEPR
MKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGG
NVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPY
IDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVE
GDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVL
EKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIAT
AALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVE
EGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTP
VTILDPKCTAKTFPDYFEQLARISQAA
Description


Functional site

1) chain A
residue 22
type
sequence K
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

2) chain A
residue 23
type
sequence S
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

3) chain A
residue 27
type
sequence R
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

4) chain A
residue 97
type
sequence I
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

5) chain A
residue 169
type
sequence S
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

6) chain A
residue 170
type
sequence S
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

7) chain A
residue 171
type
sequence Q
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

8) chain A
residue 197
type
sequence S
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

9) chain A
residue 200
type
sequence Y
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

10) chain A
residue 313
type
sequence D
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

11) chain A
residue 336
type
sequence N
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

12) chain A
residue 340
type
sequence K
description BINDING SITE FOR RESIDUE S3P A 428
source : AC1

13) chain A
residue 380
type
sequence A
description BINDING SITE FOR RESIDUE FMT A 429
source : AC2

14) chain A
residue 382
type
sequence Y
description BINDING SITE FOR RESIDUE FMT A 429
source : AC2

15) chain A
residue 22
type
sequence K
description BINDING SITE FOR RESIDUE FMT A 430
source : AC3

16) chain A
residue 313
type
sequence D
description BINDING SITE FOR RESIDUE FMT A 430
source : AC3

17) chain A
residue 341
type
sequence E
description BINDING SITE FOR RESIDUE FMT A 430
source : AC3

18) chain A
residue 344
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 430
source : AC3

19) chain A
residue 385
type
sequence H
description BINDING SITE FOR RESIDUE FMT A 430
source : AC3

20) chain A
residue 386
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 430
source : AC3

21) chain A
residue 373
type
sequence K
description BINDING SITE FOR RESIDUE FMT A 431
source : AC4

22) chain A
residue 374
type
sequence L
description BINDING SITE FOR RESIDUE FMT A 431
source : AC4

23) chain A
residue 397
type
sequence S
description BINDING SITE FOR RESIDUE FMT A 431
source : AC4

24) chain A
residue 398
type
sequence D
description BINDING SITE FOR RESIDUE FMT A 431
source : AC4

25) chain A
residue 65
type
sequence T
description BINDING SITE FOR RESIDUE FMT A 432
source : AC5

26) chain A
residue 66
type
sequence L
description BINDING SITE FOR RESIDUE FMT A 432
source : AC5

27) chain A
residue 67
type
sequence S
description BINDING SITE FOR RESIDUE FMT A 432
source : AC5

28) chain A
residue 72
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 432
source : AC5

29) chain A
residue 298
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 433
source : AC6

30) chain A
residue 300
type
sequence E
description BINDING SITE FOR RESIDUE FMT A 433
source : AC6

31) chain A
residue 301
type
sequence L
description BINDING SITE FOR RESIDUE FMT A 433
source : AC6

32) chain A
residue 324
type
sequence F
description BINDING SITE FOR RESIDUE FMT A 433
source : AC6

33) chain A
residue 58
type
sequence T
description BINDING SITE FOR RESIDUE FMT A 434
source : AC7

34) chain A
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE FMT A 434
source : AC7

35) chain A
residue 63
type
sequence S
description BINDING SITE FOR RESIDUE FMT A 434
source : AC7

36) chain A
residue 64
type
sequence Y
description BINDING SITE FOR RESIDUE FMT A 434
source : AC7

37) chain A
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE FMT A 435
source : AC8

38) chain A
residue 143
type
sequence L
description BINDING SITE FOR RESIDUE FMT A 435
source : AC8

39) chain A
residue 152
type
sequence R
description BINDING SITE FOR RESIDUE FMT A 435
source : AC8

40) chain A
residue 376
type
sequence F
description BINDING SITE FOR RESIDUE FMT A 435
source : AC8

41) chain A
residue 402
type
sequence T
description BINDING SITE FOR RESIDUE FMT A 435
source : AC8

42) chain A
residue 38
type
sequence K
description BINDING SITE FOR RESIDUE FMT A 437
source : BC1

43) chain A
residue 363
type
sequence H
description BINDING SITE FOR RESIDUE FMT A 437
source : BC1

44) chain A
residue 49
type catalytic
sequence D
description 457
source MCSA : MCSA1

45) chain A
residue 94
type catalytic
sequence N
description 457
source MCSA : MCSA1

46) chain A
residue 313
type catalytic
sequence D
description 457
source MCSA : MCSA1

47) chain A
residue 341
type catalytic
sequence E
description 457
source MCSA : MCSA1

48) chain A
residue 385
type catalytic
sequence H
description 457
source MCSA : MCSA1

49) chain A
residue 386
type catalytic
sequence R
description 457
source MCSA : MCSA1

50) chain A
residue 411
type catalytic
sequence K
description 457
source MCSA : MCSA1

51) chain A
residue 90-104
type prosite
sequence LFLGNAGIAMRSLAA
description EPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGIAMRsLaA
source prosite : PS00104

52) chain A
residue 338-356
type prosite
sequence RVKETDRLFAMATELRKVG
description EPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRLfAMateLrkVG
source prosite : PS00885

53) chain A
residue 313
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000305|PubMed:13129913
source Swiss-Prot : SWS_FT_FI1

54) chain A
residue 22
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 96
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 124
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

57) chain A
residue 171
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

58) chain A
residue 344
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

59) chain A
residue 386
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

60) chain A
residue 411
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00210
source Swiss-Prot : SWS_FT_FI2

61) chain A
residue 23
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

62) chain A
residue 27
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

63) chain A
residue 169
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

64) chain A
residue 170
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

65) chain A
residue 197
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

66) chain A
residue 313
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

67) chain A
residue 336
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

68) chain A
residue 340
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11171958, ECO:0007744|PDB:1G6S
source Swiss-Prot : SWS_FT_FI3

69) chain A
residue 408
type SITE
sequence C
description Modified by bromopyruvate => ECO:0000269|PubMed:11171958
source Swiss-Prot : SWS_FT_FI4

70) chain A
residue 411
type SITE
sequence K
description Modified by bromopyruvate => ECO:0000269|PubMed:11171958
source Swiss-Prot : SWS_FT_FI4


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