eF-site ID 1alj-AB
PDB Code 1alj
Chain A, B

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Title ALKALINE PHOSPHATASE MUTANT (H412N)
Classification HYDROLASE (PHOSPHORIC MONOESTER)
Compound ALKALINE PHOSPHATASE
Source Escherichia coli (strain K12) (PPB_ECOLI)
Sequence A:  MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAK
NIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQ
YTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD
IHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHV
TSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT
LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASL
NSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPA
VTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEG
ASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTL
VIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG
NSEEDSQENTGSQLRIAAYGPHAANVVGLTDQTDLFYTMK
AALGLK
B:  MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAK
NIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQ
YTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD
IHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHV
TSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT
LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASL
NSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPA
VTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEG
ASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTL
VIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG
NSEEDSQENTGSQLRIAAYGPHAANVVGLTDQTDLFYTMK
AALGLK
Description


Functional site

1) chain A
residue 327
type
sequence D
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

2) chain A
residue 331
type
sequence H
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

3) chain A
residue 412
type
sequence N
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

4) chain A
residue 51
type
sequence D
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

5) chain A
residue 369
type
sequence D
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

6) chain A
residue 370
type
sequence H
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

7) chain A
residue 155
type
sequence T
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

8) chain A
residue 322
type
sequence E
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

9) chain A
residue 166
type
sequence R
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

10) chain A
residue 102
type
sequence S
description CATALYTICALLY ACTIVE SITE ON A SUBUNIT
source : A

11) chain B
residue 327
type
sequence D
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

12) chain B
residue 331
type
sequence H
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

13) chain B
residue 412
type
sequence N
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

14) chain B
residue 51
type
sequence D
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

15) chain B
residue 369
type
sequence D
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

16) chain B
residue 370
type
sequence H
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

17) chain B
residue 155
type
sequence T
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

18) chain B
residue 322
type
sequence E
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

19) chain B
residue 166
type
sequence R
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

20) chain B
residue 102
type
sequence S
description CATALYTICALLY ACTIVE SITE ON B SUBUNIT
source : B

21) chain A
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 451
source : AC1

22) chain A
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE ZN A 451
source : AC1

23) chain A
residue 327
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 451
source : AC1

24) chain A
residue 369
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 451
source : AC1

25) chain A
residue 370
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 451
source : AC1

26) chain A
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE MG A 452
source : AC2

27) chain A
residue 153
type
sequence D
description BINDING SITE FOR RESIDUE MG A 452
source : AC2

28) chain A
residue 155
type
sequence T
description BINDING SITE FOR RESIDUE MG A 452
source : AC2

29) chain A
residue 322
type
sequence E
description BINDING SITE FOR RESIDUE MG A 452
source : AC2

30) chain A
residue 101
type
sequence D
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

31) chain A
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

32) chain A
residue 166
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

33) chain A
residue 327
type
sequence D
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

34) chain A
residue 331
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

35) chain A
residue 370
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

36) chain A
residue 412
type
sequence N
description BINDING SITE FOR RESIDUE PO4 A 453
source : AC3

37) chain B
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 451
source : AC4

38) chain B
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE ZN B 451
source : AC4

39) chain B
residue 327
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 451
source : AC4

40) chain B
residue 369
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 451
source : AC4

41) chain B
residue 370
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 451
source : AC4

42) chain B
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE MG B 452
source : AC5

43) chain B
residue 153
type
sequence D
description BINDING SITE FOR RESIDUE MG B 452
source : AC5

44) chain B
residue 155
type
sequence T
description BINDING SITE FOR RESIDUE MG B 452
source : AC5

45) chain B
residue 322
type
sequence E
description BINDING SITE FOR RESIDUE MG B 452
source : AC5

46) chain B
residue 101
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

47) chain B
residue 102
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

48) chain B
residue 166
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

49) chain B
residue 327
type
sequence D
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

50) chain B
residue 331
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

51) chain B
residue 370
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

52) chain B
residue 412
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 453
source : AC6

53) chain A
residue 51
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

54) chain B
residue 51
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

55) chain B
residue 153
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

56) chain B
residue 155
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

57) chain B
residue 322
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

58) chain B
residue 327
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

59) chain B
residue 331
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

60) chain B
residue 369
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

61) chain B
residue 370
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

62) chain B
residue 412
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

63) chain A
residue 153
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

64) chain A
residue 155
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

65) chain A
residue 322
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

66) chain A
residue 327
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

67) chain A
residue 331
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

68) chain A
residue 369
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

69) chain A
residue 370
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

70) chain A
residue 412
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

71) chain A
residue 102
type ACT_SITE
sequence S
description Phosphoserine intermediate
source Swiss-Prot : SWS_FT_FI1

72) chain B
residue 102
type ACT_SITE
sequence S
description Phosphoserine intermediate
source Swiss-Prot : SWS_FT_FI1

73) chain A
residue 51
type catalytic
sequence D
description 44
source MCSA : MCSA1

74) chain A
residue 369
type catalytic
sequence D
description 44
source MCSA : MCSA1

75) chain A
residue 370
type catalytic
sequence H
description 44
source MCSA : MCSA1

76) chain A
residue 412
type catalytic
sequence N
description 44
source MCSA : MCSA1

77) chain A
residue 102
type catalytic
sequence S
description 44
source MCSA : MCSA1

78) chain A
residue 153
type catalytic
sequence D
description 44
source MCSA : MCSA1

79) chain A
residue 155
type catalytic
sequence T
description 44
source MCSA : MCSA1

80) chain A
residue 166
type catalytic
sequence R
description 44
source MCSA : MCSA1

81) chain A
residue 322
type catalytic
sequence E
description 44
source MCSA : MCSA1

82) chain A
residue 327
type catalytic
sequence D
description 44
source MCSA : MCSA1

83) chain A
residue 328
type catalytic
sequence K
description 44
source MCSA : MCSA1

84) chain A
residue 331
type catalytic
sequence H
description 44
source MCSA : MCSA1

85) chain B
residue 51
type catalytic
sequence D
description 44
source MCSA : MCSA2

86) chain B
residue 369
type catalytic
sequence D
description 44
source MCSA : MCSA2

87) chain B
residue 370
type catalytic
sequence H
description 44
source MCSA : MCSA2

88) chain B
residue 412
type catalytic
sequence N
description 44
source MCSA : MCSA2

89) chain B
residue 102
type catalytic
sequence S
description 44
source MCSA : MCSA2

90) chain B
residue 153
type catalytic
sequence D
description 44
source MCSA : MCSA2

91) chain B
residue 155
type catalytic
sequence T
description 44
source MCSA : MCSA2

92) chain B
residue 166
type catalytic
sequence R
description 44
source MCSA : MCSA2

93) chain B
residue 322
type catalytic
sequence E
description 44
source MCSA : MCSA2

94) chain B
residue 327
type catalytic
sequence D
description 44
source MCSA : MCSA2

95) chain B
residue 328
type catalytic
sequence K
description 44
source MCSA : MCSA2

96) chain B
residue 331
type catalytic
sequence H
description 44
source MCSA : MCSA2

97) chain A
residue 99-107
type prosite
sequence VTDSAASAT
description ALKALINE_PHOSPHATASE Alkaline phosphatase active site. VtDSAASAT
source prosite : PS00123


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