eF-site ID 1ggf-ABCD
PDB Code 1ggf
Chain A, B, C, D
Title CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, VARIANT HIS128ASN, COMPLEX WITH HYDROGEN PEROXIDE.
Classification OXIDOREDUCTASE
Compound CATALASE HPII
Source Escherichia coli (strain K12) (CATE_ECOLI)
Sequence A:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN
SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE
DFILREKITHFDHERIPERIVNARGSAAHGYFQPYKSLSD
ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA
TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH
WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY
RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE
AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE
FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN
EQAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP
NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN
DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS
HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ
LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP
SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK
GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI
VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA
TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP
KIDKIPA
B:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN
SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE
DFILREKITHFDHERIPERIVNARGSAAHGYFQPYKSLSD
ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA
TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH
WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY
RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE
AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE
FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN
EQAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP
NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN
DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS
HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ
LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP
SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK
GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI
VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA
TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP
KIDKIPA
C:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN
SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE
DFILREKITHFDHERIPERIVNARGSAAHGYFQPYKSLSD
ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA
TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH
WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY
RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE
AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE
FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN
EQAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP
NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN
DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS
HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ
LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP
SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK
GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI
VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA
TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP
KIDKIPA
D:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN
SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE
DFILREKITHFDHERIPERIVNARGSAAHGYFQPYKSLSD
ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA
TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH
WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY
RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE
AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE
FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN
EQAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP
NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN
DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS
HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ
LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP
SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK
GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI
VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA
TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP
KIDKIPA
Description


Functional site

1) chain A
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

2) chain A
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

3) chain A
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

4) chain A
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

5) chain A
residue 165
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

6) chain A
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

7) chain A
residue 199
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

8) chain A
residue 200
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

9) chain A
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

10) chain A
residue 214
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

11) chain A
residue 274
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

12) chain A
residue 275
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

13) chain A
residue 391
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

14) chain A
residue 407
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

15) chain A
residue 410
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

16) chain A
residue 411
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

17) chain A
residue 414
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

18) chain A
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

19) chain A
residue 418
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

20) chain A
residue 419
type
sequence Q
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

21) chain A
residue 422
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

22) chain D
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE HEM A 760
source : AC1

23) chain B
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

24) chain B
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

25) chain B
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

26) chain B
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

27) chain B
residue 165
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

28) chain B
residue 199
type
sequence V
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

29) chain B
residue 200
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

30) chain B
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

31) chain B
residue 214
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

32) chain B
residue 275
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

33) chain B
residue 391
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

34) chain B
residue 407
type
sequence L
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

35) chain B
residue 411
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

36) chain B
residue 414
type
sequence S
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

37) chain B
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

38) chain B
residue 418
type
sequence T
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

39) chain B
residue 419
type
sequence Q
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

40) chain B
residue 422
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

41) chain C
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE HEM B 760
source : AC2

42) chain B
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

43) chain C
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

44) chain C
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

45) chain C
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

46) chain C
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

47) chain C
residue 165
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

48) chain C
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

49) chain C
residue 199
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

50) chain C
residue 200
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

51) chain C
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

52) chain C
residue 214
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

53) chain C
residue 275
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

54) chain C
residue 391
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

55) chain C
residue 407
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

56) chain C
residue 411
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

57) chain C
residue 414
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

58) chain C
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

59) chain C
residue 418
type
sequence T
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

60) chain C
residue 419
type
sequence Q
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

61) chain C
residue 422
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 760
source : AC3

62) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

63) chain D
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

64) chain D
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

65) chain D
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

66) chain D
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

67) chain D
residue 165
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

68) chain D
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

69) chain D
residue 199
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

70) chain D
residue 200
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

71) chain D
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

72) chain D
residue 214
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

73) chain D
residue 274
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

74) chain D
residue 275
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

75) chain D
residue 391
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

76) chain D
residue 407
type
sequence L
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

77) chain D
residue 410
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

78) chain D
residue 411
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

79) chain D
residue 414
type
sequence S
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

80) chain D
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

81) chain D
residue 418
type
sequence T
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

82) chain D
residue 419
type
sequence Q
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

83) chain D
residue 422
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 760
source : AC4

84) chain A
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE PEO A 3001
source : AC5

85) chain A
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO A 3001
source : AC5

86) chain A
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO A 3002
source : AC6

87) chain A
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PEO A 3002
source : AC6

88) chain A
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE PEO A 3002
source : AC6

89) chain A
residue 206
type
sequence F
description BINDING SITE FOR RESIDUE PEO A 3002
source : AC6

90) chain A
residue 233
type
sequence Q
description BINDING SITE FOR RESIDUE PEO A 3003
source : AC7

91) chain A
residue 234
type
sequence S
description BINDING SITE FOR RESIDUE PEO A 3003
source : AC7

92) chain A
residue 235
type
sequence A
description BINDING SITE FOR RESIDUE PEO A 3003
source : AC7

93) chain A
residue 530
type
sequence E
description BINDING SITE FOR RESIDUE PEO A 3003
source : AC7

94) chain A
residue 421
type
sequence S
description BINDING SITE FOR RESIDUE PEO D 3004
source : AC8

95) chain D
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE PEO D 3004
source : AC8

96) chain D
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE PEO D 3004
source : AC8

97) chain D
residue 120
type
sequence E
description BINDING SITE FOR RESIDUE PEO D 3004
source : AC8

98) chain D
residue 121
type
sequence R
description BINDING SITE FOR RESIDUE PEO D 3004
source : AC8

99) chain B
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE PEO B 4002
source : AC9

100) chain B
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO B 4002
source : AC9

101) chain B
residue 214
type
sequence F
description BINDING SITE FOR RESIDUE PEO B 4002
source : AC9

102) chain B
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO B 4001
source : BC1

103) chain B
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PEO B 4001
source : BC1

104) chain B
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE PEO B 4001
source : BC1

105) chain B
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE PEO B 4001
source : BC1

106) chain B
residue 233
type
sequence Q
description BINDING SITE FOR RESIDUE PEO B 4003
source : BC2

107) chain B
residue 234
type
sequence S
description BINDING SITE FOR RESIDUE PEO B 4003
source : BC2

108) chain B
residue 235
type
sequence A
description BINDING SITE FOR RESIDUE PEO B 4003
source : BC2

109) chain B
residue 530
type
sequence E
description BINDING SITE FOR RESIDUE PEO B 4003
source : BC2

110) chain C
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE PEO C 5002
source : BC3

111) chain C
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO C 5002
source : BC3

112) chain C
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PEO C 5002
source : BC3

113) chain C
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO C 5001
source : BC4

114) chain C
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PEO C 5001
source : BC4

115) chain C
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE PEO C 5001
source : BC4

116) chain C
residue 206
type
sequence F
description BINDING SITE FOR RESIDUE PEO C 5001
source : BC4

117) chain C
residue 233
type
sequence Q
description BINDING SITE FOR RESIDUE PEO C 5003
source : BC5

118) chain C
residue 234
type
sequence S
description BINDING SITE FOR RESIDUE PEO C 5003
source : BC5

119) chain C
residue 235
type
sequence A
description BINDING SITE FOR RESIDUE PEO C 5003
source : BC5

120) chain C
residue 304
type
sequence W
description BINDING SITE FOR RESIDUE PEO C 5003
source : BC5

121) chain C
residue 530
type
sequence E
description BINDING SITE FOR RESIDUE PEO C 5003
source : BC5

122) chain D
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE PEO D 6001
source : BC6

123) chain D
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO D 6001
source : BC6

124) chain D
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PEO D 6001
source : BC6

125) chain D
residue 128
type
sequence N
description BINDING SITE FOR RESIDUE PEO D 6002
source : BC7

126) chain D
residue 169
type
sequence V
description BINDING SITE FOR RESIDUE PEO D 6002
source : BC7

127) chain D
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE PEO D 6002
source : BC7

128) chain D
residue 206
type
sequence F
description BINDING SITE FOR RESIDUE PEO D 6002
source : BC7

129) chain D
residue 233
type
sequence Q
description BINDING SITE FOR RESIDUE PEO D 6003
source : BC8

130) chain D
residue 234
type
sequence S
description BINDING SITE FOR RESIDUE PEO D 6003
source : BC8

131) chain D
residue 235
type
sequence A
description BINDING SITE FOR RESIDUE PEO D 6003
source : BC8

132) chain D
residue 304
type
sequence W
description BINDING SITE FOR RESIDUE PEO D 6003
source : BC8

133) chain D
residue 530
type
sequence E
description BINDING SITE FOR RESIDUE PEO D 6003
source : BC8

134) chain A
residue 128
type catalytic
sequence N
description 573
source MCSA : MCSA1

135) chain A
residue 201
type catalytic
sequence N
description 573
source MCSA : MCSA1

136) chain A
residue 392
type catalytic
sequence H
description 573
source MCSA : MCSA1

137) chain B
residue 128
type catalytic
sequence N
description 573
source MCSA : MCSA2

138) chain B
residue 201
type catalytic
sequence N
description 573
source MCSA : MCSA2

139) chain B
residue 392
type catalytic
sequence H
description 573
source MCSA : MCSA2

140) chain C
residue 128
type catalytic
sequence N
description 573
source MCSA : MCSA3

141) chain C
residue 201
type catalytic
sequence N
description 573
source MCSA : MCSA3

142) chain C
residue 392
type catalytic
sequence H
description 573
source MCSA : MCSA3

143) chain D
residue 128
type catalytic
sequence N
description 573
source MCSA : MCSA4

144) chain D
residue 201
type catalytic
sequence N
description 573
source MCSA : MCSA4

145) chain D
residue 392
type catalytic
sequence H
description 573
source MCSA : MCSA4

146) chain A
residue 128
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

147) chain A
residue 201
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

148) chain B
residue 128
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

149) chain B
residue 201
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

150) chain C
residue 128
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

151) chain C
residue 201
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

152) chain D
residue 128
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

153) chain D
residue 201
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

154) chain A
residue 392
type CROSSLNK
sequence H
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

155) chain A
residue 415
type CROSSLNK
sequence Y
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

156) chain B
residue 392
type CROSSLNK
sequence H
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

157) chain B
residue 415
type CROSSLNK
sequence Y
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

158) chain C
residue 392
type CROSSLNK
sequence H
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

159) chain C
residue 415
type CROSSLNK
sequence Y
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

160) chain D
residue 392
type CROSSLNK
sequence H
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

161) chain D
residue 415
type CROSSLNK
sequence Y
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

162) chain A
residue 415
type BINDING
sequence Y
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

163) chain B
residue 415
type BINDING
sequence Y
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

164) chain C
residue 415
type BINDING
sequence Y
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

165) chain D
residue 415
type BINDING
sequence Y
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

166) chain A
residue 411-419
type prosite
sequence RLFSYTDTQ
description CATALASE_1 Catalase proximal heme-ligand signature. RLFSYtDTQ
source prosite : PS00437


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