eF-site ID 1mpy-ABCD
PDB Code 1mpy
Chain A, B, C, D

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Title STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2
Classification OXIDOREDUCTASE
Compound CATECHOL 2,3-DIOXYGENASE
Source Pseudomonas putida (Arthrobacter siderocapsulatus) (XYLE1_PSEPU)
Sequence A:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG
RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ
LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY
ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE
LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD
VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID
IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV
TWTTDQLGKAIFYHDRILNERFMTVLT
B:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG
RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ
LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY
ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE
LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD
VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID
IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV
TWTTDQLGKAIFYHDRILNERFMTVLT
C:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG
RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ
LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY
ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE
LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD
VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID
IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV
TWTTDQLGKAIFYHDRILNERFMTVLT
D:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG
RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ
LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY
ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE
LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD
VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID
IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV
TWTTDQLGKAIFYHDRILNERFMTVLT
Description


Functional site

1) chain A
residue 153
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 308
source : AC1

2) chain A
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 308
source : AC1

3) chain A
residue 216
type
sequence S
description BINDING SITE FOR RESIDUE FE2 A 308
source : AC1

4) chain A
residue 265
type
sequence E
description BINDING SITE FOR RESIDUE FE2 A 308
source : AC1

5) chain B
residue 153
type
sequence H
description BINDING SITE FOR RESIDUE FE2 B 308
source : AC2

6) chain B
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FE2 B 308
source : AC2

7) chain B
residue 216
type
sequence S
description BINDING SITE FOR RESIDUE FE2 B 308
source : AC2

8) chain B
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE FE2 B 308
source : AC2

9) chain B
residue 265
type
sequence E
description BINDING SITE FOR RESIDUE FE2 B 308
source : AC2

10) chain C
residue 153
type
sequence H
description BINDING SITE FOR RESIDUE FE2 C 308
source : AC3

11) chain C
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FE2 C 308
source : AC3

12) chain C
residue 216
type
sequence S
description BINDING SITE FOR RESIDUE FE2 C 308
source : AC3

13) chain C
residue 265
type
sequence E
description BINDING SITE FOR RESIDUE FE2 C 308
source : AC3

14) chain D
residue 153
type
sequence H
description BINDING SITE FOR RESIDUE FE2 D 308
source : AC4

15) chain D
residue 214
type
sequence H
description BINDING SITE FOR RESIDUE FE2 D 308
source : AC4

16) chain D
residue 216
type
sequence S
description BINDING SITE FOR RESIDUE FE2 D 308
source : AC4

17) chain D
residue 265
type
sequence E
description BINDING SITE FOR RESIDUE FE2 D 308
source : AC4

18) chain A
residue 191
type
sequence F
description BINDING SITE FOR RESIDUE ACN A 309
source : AC5

19) chain A
residue 246
type
sequence H
description BINDING SITE FOR RESIDUE ACN A 309
source : AC5

20) chain A
residue 248
type
sequence L
description BINDING SITE FOR RESIDUE ACN A 309
source : AC5

21) chain A
residue 249
type
sequence T
description BINDING SITE FOR RESIDUE ACN A 309
source : AC5

22) chain A
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE ACN A 309
source : AC5

23) chain B
residue 246
type
sequence H
description BINDING SITE FOR RESIDUE ACN B 309
source : AC6

24) chain B
residue 248
type
sequence L
description BINDING SITE FOR RESIDUE ACN B 309
source : AC6

25) chain B
residue 249
type
sequence T
description BINDING SITE FOR RESIDUE ACN B 309
source : AC6

26) chain B
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE ACN B 309
source : AC6

27) chain C
residue 246
type
sequence H
description BINDING SITE FOR RESIDUE ACN C 309
source : AC7

28) chain C
residue 248
type
sequence L
description BINDING SITE FOR RESIDUE ACN C 309
source : AC7

29) chain C
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE ACN C 309
source : AC7

30) chain D
residue 155
type
sequence L
description BINDING SITE FOR RESIDUE ACN D 309
source : AC8

31) chain D
residue 246
type
sequence H
description BINDING SITE FOR RESIDUE ACN D 309
source : AC8

32) chain D
residue 255
type
sequence Y
description BINDING SITE FOR RESIDUE ACN D 309
source : AC8

33) chain D
residue 291
type
sequence I
description BINDING SITE FOR RESIDUE ACN D 309
source : AC8

34) chain A
residue 153
type catalytic
sequence H
description 34
source MCSA : MCSA1

35) chain A
residue 199
type catalytic
sequence H
description 34
source MCSA : MCSA1

36) chain A
residue 214
type catalytic
sequence H
description 34
source MCSA : MCSA1

37) chain A
residue 246
type catalytic
sequence H
description 34
source MCSA : MCSA1

38) chain A
residue 255
type catalytic
sequence Y
description 34
source MCSA : MCSA1

39) chain A
residue 265
type catalytic
sequence E
description 34
source MCSA : MCSA1

40) chain B
residue 153
type catalytic
sequence H
description 34
source MCSA : MCSA2

41) chain B
residue 199
type catalytic
sequence H
description 34
source MCSA : MCSA2

42) chain B
residue 214
type catalytic
sequence H
description 34
source MCSA : MCSA2

43) chain B
residue 246
type catalytic
sequence H
description 34
source MCSA : MCSA2

44) chain B
residue 255
type catalytic
sequence Y
description 34
source MCSA : MCSA2

45) chain B
residue 265
type catalytic
sequence E
description 34
source MCSA : MCSA2

46) chain C
residue 153
type catalytic
sequence H
description 34
source MCSA : MCSA3

47) chain C
residue 199
type catalytic
sequence H
description 34
source MCSA : MCSA3

48) chain C
residue 214
type catalytic
sequence H
description 34
source MCSA : MCSA3

49) chain C
residue 246
type catalytic
sequence H
description 34
source MCSA : MCSA3

50) chain C
residue 255
type catalytic
sequence Y
description 34
source MCSA : MCSA3

51) chain C
residue 265
type catalytic
sequence E
description 34
source MCSA : MCSA3

52) chain D
residue 153
type catalytic
sequence H
description 34
source MCSA : MCSA4

53) chain D
residue 199
type catalytic
sequence H
description 34
source MCSA : MCSA4

54) chain D
residue 214
type catalytic
sequence H
description 34
source MCSA : MCSA4

55) chain D
residue 246
type catalytic
sequence H
description 34
source MCSA : MCSA4

56) chain D
residue 255
type catalytic
sequence Y
description 34
source MCSA : MCSA4

57) chain D
residue 265
type catalytic
sequence E
description 34
source MCSA : MCSA4

58) chain A
residue 244-265
type prosite
sequence TRHGLTHGKTIYFFDPSGNRNE
description EXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. TrHglthgktIYffDPsGnrnE
source prosite : PS00082

59) chain A
residue 153
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

60) chain D
residue 153
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

61) chain D
residue 214
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

62) chain D
residue 265
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

63) chain A
residue 214
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 265
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

65) chain B
residue 153
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

66) chain B
residue 214
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

67) chain B
residue 265
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1

68) chain C
residue 153
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

69) chain C
residue 214
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

70) chain C
residue 265
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI1


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