eF-site ID 5aeu-ABCDEFGH
PDB Code 5aeu
Chain A, B, C, D, E, F, G, H

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Title Crystal structure of II9 variant of Biphenyl dioxygenase from Burkholderia xenovorans LB400
Classification OXIDOREDUCTASE
Compound BIPHENYL DIOXYGENASE SUBUNIT ALPHA
Source (BPHE_BURXL)
Sequence A:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS
WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL
NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP
FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY
LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ
FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR
AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE
QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG
PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ
DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP
GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP
B:  PHFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEA
WFALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDET
HETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATP
DTFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGF
SIAKRTILLDASTLLSNNLSMFF
C:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS
WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL
NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP
FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY
LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ
FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR
AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE
QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG
PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ
DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP
GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP
D:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW
FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH
ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD
TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS
IAKRTILLDASTLLSNNLSMFF
E:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS
WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL
NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP
FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY
LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ
FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR
AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE
QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG
PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ
DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP
GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP
F:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW
FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH
ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD
TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS
IAKRTILLDASTLLSNNLSMFF
G:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS
WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL
NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP
FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY
LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ
FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR
AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE
QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG
PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ
DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP
GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP
H:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW
FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH
ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD
TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS
IAKRTILLDASTLLSNNLSMFF
Description


Functional site

1) chain A
residue 100
type
sequence C
description BINDING SITE FOR RESIDUE FES A 500
source : AC1

2) chain A
residue 102
type
sequence H
description BINDING SITE FOR RESIDUE FES A 500
source : AC1

3) chain A
residue 103
type
sequence R
description BINDING SITE FOR RESIDUE FES A 500
source : AC1

4) chain A
residue 120
type
sequence C
description BINDING SITE FOR RESIDUE FES A 500
source : AC1

5) chain A
residue 123
type
sequence H
description BINDING SITE FOR RESIDUE FES A 500
source : AC1

6) chain A
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE FES A 500
source : AC1

7) chain A
residue 226
type
sequence Q
description BINDING SITE FOR RESIDUE FE2 A 501
source : AC2

8) chain A
residue 233
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 501
source : AC2

9) chain A
residue 239
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 501
source : AC2

10) chain A
residue 388
type
sequence D
description BINDING SITE FOR RESIDUE FE2 A 501
source : AC2

11) chain C
residue 100
type
sequence C
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

12) chain C
residue 102
type
sequence H
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

13) chain C
residue 103
type
sequence R
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

14) chain C
residue 120
type
sequence C
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

15) chain C
residue 123
type
sequence H
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

16) chain C
residue 124
type
sequence G
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

17) chain C
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE FES C 500
source : AC3

18) chain C
residue 226
type
sequence Q
description BINDING SITE FOR RESIDUE FE2 C 501
source : AC4

19) chain C
residue 233
type
sequence H
description BINDING SITE FOR RESIDUE FE2 C 501
source : AC4

20) chain C
residue 239
type
sequence H
description BINDING SITE FOR RESIDUE FE2 C 501
source : AC4

21) chain C
residue 388
type
sequence D
description BINDING SITE FOR RESIDUE FE2 C 501
source : AC4

22) chain E
residue 100
type
sequence C
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

23) chain E
residue 102
type
sequence H
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

24) chain E
residue 103
type
sequence R
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

25) chain E
residue 120
type
sequence C
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

26) chain E
residue 122
type
sequence Y
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

27) chain E
residue 123
type
sequence H
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

28) chain E
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE FES E 500
source : AC5

29) chain E
residue 226
type
sequence Q
description BINDING SITE FOR RESIDUE FE2 E 501
source : AC6

30) chain E
residue 233
type
sequence H
description BINDING SITE FOR RESIDUE FE2 E 501
source : AC6

31) chain E
residue 239
type
sequence H
description BINDING SITE FOR RESIDUE FE2 E 501
source : AC6

32) chain E
residue 388
type
sequence D
description BINDING SITE FOR RESIDUE FE2 E 501
source : AC6

33) chain G
residue 100
type
sequence C
description BINDING SITE FOR RESIDUE FES G 500
source : AC7

34) chain G
residue 102
type
sequence H
description BINDING SITE FOR RESIDUE FES G 500
source : AC7

35) chain G
residue 103
type
sequence R
description BINDING SITE FOR RESIDUE FES G 500
source : AC7

36) chain G
residue 120
type
sequence C
description BINDING SITE FOR RESIDUE FES G 500
source : AC7

37) chain G
residue 123
type
sequence H
description BINDING SITE FOR RESIDUE FES G 500
source : AC7

38) chain G
residue 125
type
sequence W
description BINDING SITE FOR RESIDUE FES G 500
source : AC7

39) chain G
residue 226
type
sequence Q
description BINDING SITE FOR RESIDUE FE2 G 501
source : AC8

40) chain G
residue 233
type
sequence H
description BINDING SITE FOR RESIDUE FE2 G 501
source : AC8

41) chain G
residue 239
type
sequence H
description BINDING SITE FOR RESIDUE FE2 G 501
source : AC8

42) chain G
residue 388
type
sequence D
description BINDING SITE FOR RESIDUE FE2 G 501
source : AC8

43) chain A
residue 100-123
type prosite
sequence CRHRGMRICRSDAGNAKAFTCSYH
description RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH
source prosite : PS00570

44) chain A
residue 100
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

45) chain E
residue 102
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

46) chain E
residue 120
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

47) chain E
residue 123
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

48) chain G
residue 100
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

49) chain G
residue 102
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

50) chain G
residue 120
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

51) chain G
residue 123
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

52) chain A
residue 102
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 120
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

54) chain A
residue 123
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

55) chain C
residue 100
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

56) chain C
residue 102
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

57) chain C
residue 120
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

58) chain C
residue 123
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

59) chain E
residue 100
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI1

60) chain A
residue 233
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

61) chain A
residue 239
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

62) chain C
residue 233
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

63) chain C
residue 239
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

64) chain E
residue 233
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

65) chain E
residue 239
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

66) chain G
residue 233
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

67) chain G
residue 239
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2


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