eF-site ID 1bl9-AB
PDB Code 1bl9
Chain A, B

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Title CONFORMATIONAL CHANGES OCCURRING UPON REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA
Classification OXIDOREDUCTASE
Compound NITRITE REDUCTASE
Source ORGANISM_SCIENTIFIC: Pseudomonas aeruginosa;
Sequence A:  AEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQR
CAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPL
GMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRE
SWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDG
DSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMID
LWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYW
PPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAII
ASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSIGAAPFL
HDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGK
TPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHP
QYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDAR
ISQSVAVFDLKNLDAKYQVLPIAEWADLGEGAKRVVQPEY
NKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAVVKDPRL
ITPTGKFNVYNTQHDVY
B:  AEQYQGAASAVDPAHVVRTNGAPDMSESEFNEAKQIYFQR
CAGCHGVLRKGATGKPLTPDITQQRGQQYLEALITYGTPL
GMPNWGSSGELSKEQITLMAKYIQHTPPQPPEWGMPEMRE
SWKVLVKPEDRPKKQLNDLDLPNLFSVTLRDAGQIALVDG
DSKKIVKVIDTGYAVHISRMSASGRYLLVIGRDARIDMID
LWAKEPTKVAEIKIGIEARSVESSKFKGYEDRYTIAGAYW
PPQFAIMDGETLEPKQIVSTRGMTVDTQTYHPEPRVAAII
ASHEHPEFIVNVKETGKVLLVNYKDIDNLTVTSIGAAPFL
HDGGWDSSHRYFMTAANNSNKVAVIDSKDRRLSALVDVGK
TPHPGRGANFVHPKYGPVWSTSHLGDGSISLIGTDPKNHP
QYAWKKVAELQGQGGGSLFIKTHPKSSHLYVDTTFNPDAR
ISQSVAVFDLKNLDAKYQVLPIAEWADLGEGAKRVVQPEY
NKRGDEVWFSVWNGKNDSSALVVVDDKTLKLKAVVKDPRL
ITPTGKFNVYNTQHDVY
Description (1)  NITRITE REDUCTASE, HEME C, HEME D


Functional site

1) chain A
residue 327
type
sequence H
description CATALYTIC SITE ON SUBUNIT A
source : CSA

2) chain A
residue 369
type
sequence H
description CATALYTIC SITE ON SUBUNIT A
source : CSA

3) chain B
residue 327
type
sequence H
description CATALYTIC SITE ON SUBUNIT B
source : CSB

4) chain B
residue 369
type
sequence H
description CATALYTIC SITE ON SUBUNIT B
source : CSB

5) chain B
residue 369
type
sequence H
description BINDING SITE FOR RESIDUE OH B 603
source : AC1

6) chain A
residue 46
type
sequence R
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

7) chain A
residue 47
type
sequence C
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

8) chain A
residue 50
type
sequence C
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

9) chain A
residue 51
type
sequence H
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

10) chain A
residue 59
type
sequence T
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

11) chain A
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

12) chain A
residue 61
type
sequence K
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

13) chain A
residue 71
type
sequence R
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

14) chain A
residue 76
type
sequence L
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

15) chain A
residue 79
type
sequence L
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

16) chain A
residue 84
type
sequence T
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

17) chain A
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

18) chain A
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

19) chain A
residue 88
type
sequence M
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

20) chain A
residue 89
type
sequence P
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

21) chain A
residue 91
type
sequence W
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

22) chain B
residue 8
type
sequence E
description BINDING SITE FOR RESIDUE HEC A 601
source : AC2

23) chain A
residue 156
type
sequence R
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

24) chain A
residue 182
type
sequence H
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

25) chain A
residue 183
type
sequence I
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

26) chain A
residue 185
type
sequence R
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

27) chain A
residue 198
type
sequence R
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

28) chain A
residue 225
type
sequence R
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

29) chain A
residue 226
type
sequence S
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

30) chain A
residue 245
type
sequence Y
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

31) chain A
residue 283
type
sequence A
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

32) chain A
residue 284
type
sequence A
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

33) chain A
residue 285
type
sequence I
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

34) chain A
residue 327
type
sequence H
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

35) chain A
residue 372
type
sequence R
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

36) chain A
residue 425
type
sequence F
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

37) chain A
residue 483
type
sequence Q
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

38) chain A
residue 531
type
sequence G
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

39) chain A
residue 533
type
sequence F
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

40) chain B
residue 10
type
sequence Y
description BINDING SITE FOR RESIDUE DHE A 602
source : AC3

41) chain A
residue 8
type
sequence E
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

42) chain B
residue 46
type
sequence R
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

43) chain B
residue 47
type
sequence C
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

44) chain B
residue 50
type
sequence C
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

45) chain B
residue 51
type
sequence H
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

46) chain B
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

47) chain B
residue 61
type
sequence K
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

48) chain B
residue 63
type
sequence L
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

49) chain B
residue 71
type
sequence R
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

50) chain B
residue 84
type
sequence T
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

51) chain B
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

52) chain B
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

53) chain B
residue 88
type
sequence M
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

54) chain B
residue 89
type
sequence P
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

55) chain B
residue 91
type
sequence W
description BINDING SITE FOR RESIDUE HEC B 601
source : AC4

56) chain A
residue 10
type
sequence Y
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

57) chain A
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

58) chain B
residue 156
type
sequence R
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

59) chain B
residue 182
type
sequence H
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

60) chain B
residue 183
type
sequence I
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

61) chain B
residue 185
type
sequence R
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

62) chain B
residue 198
type
sequence R
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

63) chain B
residue 225
type
sequence R
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

64) chain B
residue 226
type
sequence S
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

65) chain B
residue 245
type
sequence Y
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

66) chain B
residue 283
type
sequence A
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

67) chain B
residue 284
type
sequence A
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

68) chain B
residue 285
type
sequence I
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

69) chain B
residue 327
type
sequence H
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

70) chain B
residue 372
type
sequence R
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

71) chain B
residue 425
type
sequence F
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

72) chain B
residue 483
type
sequence Q
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

73) chain B
residue 498
type
sequence W
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

74) chain B
residue 531
type
sequence G
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

75) chain B
residue 533
type
sequence F
description BINDING SITE FOR RESIDUE DHE B 602
source : AC5

76) chain A
residue 47
type BINDING
sequence C
description covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI1

77) chain A
residue 50
type BINDING
sequence C
description covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI1

78) chain B
residue 47
type BINDING
sequence C
description covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI1

79) chain B
residue 50
type BINDING
sequence C
description covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI1

80) chain A
residue 51
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI2

81) chain A
residue 88
type BINDING
sequence M
description axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI2

82) chain B
residue 51
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI2

83) chain B
residue 88
type BINDING
sequence M
description axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI2

84) chain A
residue 47
type catalytic
sequence C
description 903
source MCSA : MCSA1

85) chain A
residue 50
type catalytic
sequence C
description 903
source MCSA : MCSA1

86) chain A
residue 51
type catalytic
sequence H
description 903
source MCSA : MCSA1

87) chain A
residue 88
type catalytic
sequence M
description 903
source MCSA : MCSA1

88) chain A
residue 327
type catalytic
sequence H
description 903
source MCSA : MCSA1

89) chain A
residue 369
type catalytic
sequence H
description 903
source MCSA : MCSA1

90) chain B
residue 47
type catalytic
sequence C
description 903
source MCSA : MCSA2

91) chain B
residue 50
type catalytic
sequence C
description 903
source MCSA : MCSA2

92) chain B
residue 51
type catalytic
sequence H
description 903
source MCSA : MCSA2

93) chain B
residue 88
type catalytic
sequence M
description 903
source MCSA : MCSA2

94) chain B
residue 327
type catalytic
sequence H
description 903
source MCSA : MCSA2

95) chain B
residue 369
type catalytic
sequence H
description 903
source MCSA : MCSA2

96) chain A
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

97) chain B
residue 225
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

98) chain B
residue 226
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

99) chain B
residue 245
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

100) chain B
residue 372
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

101) chain B
residue 483
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

102) chain A
residue 84
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

103) chain A
residue 225
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

104) chain A
residue 226
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

105) chain A
residue 245
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

106) chain A
residue 372
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

107) chain A
residue 483
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

108) chain B
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

109) chain B
residue 84
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI3

110) chain A
residue 182
type BINDING
sequence H
description proximal binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI4

111) chain B
residue 182
type BINDING
sequence H
description proximal binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR
source Swiss-Prot : SWS_FT_FI4


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