eF-site ID 6o4n-A
PDB Code 6o4n
Chain A

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Title Crystal Structure of Enolase from Chlamydia trachomatis
Classification HYDROLASE
Compound Enolase
Source (ENO_CHLTB)
Sequence A:  DVVISDIEAREILDSRGYPTLCVKVITNTGTFGEACVPSG
ASTGIKEALELRDKDPKRYQGKGVLQAISNVEKVLVPALQ
GFSVFDQITADAIMIDADGTPNKEKLGANAILGVSLALAK
AAANTLQRPLYRYLGGSFSHVLPCPMMNLINGGMHATNGL
QFQEFMIRPISAPSLKEAVRMGAEVFNALKKILQNRQLAT
GVGDEGGFAPNLASNAEALDLLLTAIETAGFTPREDISLA
LDCAASSFYNTQDKTYDGKSYADQVGILAELCEHYPIDSI
EDGLAEEDFEGWKLLSETLGDRVQLVGDDLFVTNSALIAE
GIAQGLANAVLIKPNQIGTLTETAEAIRLATIQGYATILS
HRSGETEDTTIADLAVAFNTGQIKTGSLSRSERIAKYNRL
MAIEEEMGPEALFQDSNPFSKA
Description


Functional site

1) chain A
residue 48
type
sequence K
description binding site for residue MRD A 501
source : AC1

2) chain A
residue 289
type
sequence E
description binding site for residue MRD A 501
source : AC1

3) chain A
residue 291
type
sequence F
description binding site for residue MRD A 501
source : AC1

4) chain A
residue 312
type
sequence L
description binding site for residue MRD A 501
source : AC1

5) chain A
residue 319
type
sequence L
description binding site for residue MRD A 501
source : AC1

6) chain A
residue 322
type
sequence E
description binding site for residue MRD A 501
source : AC1

7) chain A
residue 326
type
sequence Q
description binding site for residue MRD A 501
source : AC1

8) chain A
residue 56
type
sequence K
description binding site for residue EDO A 502
source : AC2

9) chain A
residue 63
type
sequence G
description binding site for residue EDO A 502
source : AC2

10) chain A
residue 68
type
sequence Q
description binding site for residue EDO A 503
source : AC3

11) chain A
residue 42
type
sequence G
description binding site for residue PO4 A 504
source : AC4

12) chain A
residue 43
type
sequence A
description binding site for residue PO4 A 504
source : AC4

13) chain A
residue 44
type
sequence S
description binding site for residue PO4 A 504
source : AC4

14) chain A
residue 157
type
sequence H
description binding site for residue PO4 A 504
source : AC4

15) chain A
residue 165
type
sequence Q
description binding site for residue PO4 A 504
source : AC4

16) chain A
residue 335
type
sequence K
description binding site for residue PO4 A 504
source : AC4

17) chain A
residue 364
type
sequence R
description binding site for residue PO4 A 504
source : AC4

18) chain A
residue 365
type
sequence S
description binding site for residue PO4 A 504
source : AC4

19) chain A
residue 44
type
sequence S
description binding site for residue MG A 505
source : AC5

20) chain A
residue 244
type
sequence D
description binding site for residue MG A 506
source : AC6

21) chain A
residue 283
type
sequence E
description binding site for residue MG A 506
source : AC6

22) chain A
residue 310
type
sequence D
description binding site for residue MG A 506
source : AC6

23) chain A
residue 335
type
sequence K
description binding site for residue MG A 506
source : AC6

24) chain A
residue 386
type
sequence K
description binding site for residue MG A 506
source : AC6

25) chain A
residue 12
type
sequence R
description binding site for residue MRD A 507
source : AC7

26) chain A
residue 36
type
sequence E
description binding site for residue MRD A 507
source : AC7

27) chain A
residue 38
type
sequence C
description binding site for residue MRD A 507
source : AC7

28) chain A
residue 369
type
sequence E
description binding site for residue MRD A 507
source : AC7

29) chain A
residue 370
type
sequence D
description binding site for residue MRD A 507
source : AC7

30) chain A
residue 101
type
sequence G
description binding site for residue EDO A 508
source : AC8

31) chain A
residue 102
type
sequence T
description binding site for residue EDO A 508
source : AC8

32) chain A
residue 357
type
sequence Y
description binding site for residue EDO A 509
source : AC9

33) chain A
residue 163
type
sequence Q
description binding site for residue EDO A 510
source : AD1

34) chain A
residue 216
type
sequence S
description binding site for residue EDO A 510
source : AD1

35) chain A
residue 217
type
sequence N
description binding site for residue EDO A 510
source : AD1

36) chain A
residue 45
type
sequence T
description binding site for residue MG A 511
source : AD2

37) chain A
residue 201
type
sequence A
description binding site for residue CL A 512
source : AD3

38) chain A
residue 213
type
sequence N
description binding site for residue CL A 512
source : AD3

39) chain A
residue 213
type
sequence N
description binding site for residue EDO A 513
source : AD4

40) chain A
residue 199
type
sequence Q
description binding site for residue EDO B 1601
source : AD5

41) chain A
residue 200
type
sequence L
description binding site for residue EDO B 1601
source : AD5

42) chain A
residue 201
type
sequence A
description binding site for residue EDO B 1601
source : AD5

43) chain A
residue 157
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 166
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

45) chain A
residue 244
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 283
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 310
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 362
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

49) chain A
residue 386
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI3

50) chain A
residue 207
type ACT_SITE
sequence E
description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI1

51) chain A
residue 335
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 335
type BINDING
sequence K
description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318
source Swiss-Prot : SWS_FT_FI4

53) chain A
residue 332-345
type prosite
sequence VLIKPNQIGTLTET
description ENOLASE Enolase signature. VLIKpNQIGTLTET
source prosite : PS00164


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