eF-site ID 2gc4-IJKLMNOP
PDB Code 2gc4
Chain I, J, K, L, M, N, O, P

click to enlarge
Title Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.
Classification Oxidoreductase, Electron transport
Compound Methylamine dehydrogenase heavy chain
Source ORGANISM_SCIENTIFIC: Paracoccus denitrificans;
Sequence I:  EAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDA
RRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPV
VADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTAD
IELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGV
VDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKV
AFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPT
YTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQ
VAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERL
AKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESG
EELRSVNQLGHGPQVITTADMG
J:  TDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNC
PPGTKLATASXVASCYNPTDGQSYLIAYRDCCGYNVSGRC
PCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPI
VGKAS
K:  DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVG
DTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSL
TFTEAGTYDYHCTPHPFMRGKVVVE
L:  APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYN
EDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTY
PGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWV
RHLYTGDPKDASWLTDEQKAGFTPFQP
M:  EAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDA
RRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPV
VADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTAD
IELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGV
VDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKV
AFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPT
YTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQ
VAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERL
AKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESG
EELRSVNQLGHGPQVITTADMG
N:  TDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNC
PPGTKLATASXVASCYNPTDGQSYLIAYRDCCGYNVSGRC
PCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPI
VGKAS
O:  DKATIPSESPFAAAEVADGAIVVDIAKMKYETPELHVKVG
DTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSL
TFTEAGTYDYHCTPHPFMRGKVVVE
P:  APQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENVYN
EDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTY
PGNETDVGLFSTLYGGATGQMGPMWGSLTLDEMLRTMAWV
RHLYTGDPKDASWLTDEQKAGFTPFQP
Description


Functional site

1) chain K
residue 53
type
sequence H
description BINDING SITE FOR RESIDUE CU K 107
source : AC2

2) chain K
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE CU K 107
source : AC2

3) chain K
residue 95
type
sequence H
description BINDING SITE FOR RESIDUE CU K 107
source : AC2

4) chain K
residue 98
type
sequence M
description BINDING SITE FOR RESIDUE CU K 107
source : AC2

5) chain O
residue 53
type
sequence H
description BINDING SITE FOR RESIDUE CU O 107
source : AC3

6) chain O
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE CU O 107
source : AC3

7) chain O
residue 95
type
sequence H
description BINDING SITE FOR RESIDUE CU O 107
source : AC3

8) chain O
residue 98
type
sequence M
description BINDING SITE FOR RESIDUE CU O 107
source : AC3

9) chain K
residue 31
type
sequence E
description BINDING SITE FOR RESIDUE NA L 601
source : AC5

10) chain L
residue 72
type
sequence G
description BINDING SITE FOR RESIDUE NA L 601
source : AC5

11) chain L
residue 75
type
sequence D
description BINDING SITE FOR RESIDUE NA L 601
source : AC5

12) chain L
residue 77
type
sequence Y
description BINDING SITE FOR RESIDUE NA L 601
source : AC5

13) chain O
residue 31
type
sequence E
description BINDING SITE FOR RESIDUE NA P 602
source : AC6

14) chain P
residue 72
type
sequence G
description BINDING SITE FOR RESIDUE NA P 602
source : AC6

15) chain P
residue 75
type
sequence D
description BINDING SITE FOR RESIDUE NA P 602
source : AC6

16) chain P
residue 77
type
sequence Y
description BINDING SITE FOR RESIDUE NA P 602
source : AC6

17) chain L
residue 56
type
sequence M
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

18) chain L
residue 57
type
sequence C
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

19) chain L
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

20) chain L
residue 61
type
sequence H
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

21) chain L
residue 71
type
sequence P
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

22) chain L
residue 73
type
sequence L
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

23) chain L
residue 78
type
sequence W
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

24) chain L
residue 79
type
sequence T
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

25) chain L
residue 80
type
sequence Y
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

26) chain L
residue 83
type
sequence N
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

27) chain L
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

28) chain L
residue 97
type
sequence A
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

29) chain L
residue 98
type
sequence T
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

30) chain L
residue 100
type
sequence Q
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

31) chain L
residue 101
type
sequence M
description BINDING SITE FOR RESIDUE HEC L 200
source : BC1

32) chain P
residue 56
type
sequence M
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

33) chain P
residue 57
type
sequence C
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

34) chain P
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

35) chain P
residue 61
type
sequence H
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

36) chain P
residue 71
type
sequence P
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

37) chain P
residue 73
type
sequence L
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

38) chain P
residue 78
type
sequence W
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

39) chain P
residue 79
type
sequence T
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

40) chain P
residue 80
type
sequence Y
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

41) chain P
residue 83
type
sequence N
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

42) chain P
residue 93
type
sequence L
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

43) chain P
residue 97
type
sequence A
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

44) chain P
residue 98
type
sequence T
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

45) chain P
residue 100
type
sequence Q
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

46) chain P
residue 101
type
sequence M
description BINDING SITE FOR RESIDUE HEC P 200
source : BC3

47) chain J
residue 32
type catalytic
sequence D
description 13
source MCSA : MCSA3

48) chain J
residue 57
type catalytic
sequence X
description 13
source MCSA : MCSA3

49) chain J
residue 76
type catalytic
sequence D
description 13
source MCSA : MCSA3

50) chain J
residue 108
type catalytic
sequence W
description 13
source MCSA : MCSA3

51) chain J
residue 119
type catalytic
sequence Y
description 13
source MCSA : MCSA3

52) chain J
residue 122
type catalytic
sequence T
description 13
source MCSA : MCSA3

53) chain N
residue 32
type catalytic
sequence D
description 13
source MCSA : MCSA4

54) chain N
residue 57
type catalytic
sequence X
description 13
source MCSA : MCSA4

55) chain N
residue 76
type catalytic
sequence D
description 13
source MCSA : MCSA4

56) chain N
residue 108
type catalytic
sequence W
description 13
source MCSA : MCSA4

57) chain N
residue 119
type catalytic
sequence Y
description 13
source MCSA : MCSA4

58) chain N
residue 122
type catalytic
sequence T
description 13
source MCSA : MCSA4

59) chain K
residue 92
type BINDING
sequence C
description covalent
source Swiss-Prot : SWS_FT_FI1

60) chain K
residue 95
type BINDING
sequence H
description covalent
source Swiss-Prot : SWS_FT_FI1

61) chain K
residue 98
type BINDING
sequence M
description covalent
source Swiss-Prot : SWS_FT_FI1

62) chain O
residue 53
type BINDING
sequence H
description covalent
source Swiss-Prot : SWS_FT_FI1

63) chain O
residue 92
type BINDING
sequence C
description covalent
source Swiss-Prot : SWS_FT_FI1

64) chain O
residue 95
type BINDING
sequence H
description covalent
source Swiss-Prot : SWS_FT_FI1

65) chain O
residue 98
type BINDING
sequence M
description covalent
source Swiss-Prot : SWS_FT_FI1

66) chain L
residue 57
type BINDING
sequence C
description covalent
source Swiss-Prot : SWS_FT_FI1

67) chain L
residue 60
type BINDING
sequence C
description covalent
source Swiss-Prot : SWS_FT_FI1

68) chain P
residue 57
type BINDING
sequence C
description covalent
source Swiss-Prot : SWS_FT_FI1

69) chain P
residue 60
type BINDING
sequence C
description covalent
source Swiss-Prot : SWS_FT_FI1

70) chain K
residue 53
type BINDING
sequence H
description covalent
source Swiss-Prot : SWS_FT_FI1

71) chain L
residue 61
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

72) chain P
residue 61
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

73) chain J
residue 57
type BINDING
sequence X
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

74) chain J
residue 108
type BINDING
sequence W
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

75) chain N
residue 57
type BINDING
sequence X
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

76) chain N
residue 108
type BINDING
sequence W
description axial binding residue
source Swiss-Prot : SWS_FT_FI2


Display surface

Download
Links