eF-site ID 2xiq-AB
PDB Code 2xiq
Chain A, B

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Title Crystal structure of human methylmalonyl-CoA mutase in complex with adenosylcobalamin and malonyl-CoA
Classification ISOMERASE
Compound METHYLMALONYL-COA MUTASE, MITOCHONDRIAL
Source (MUTA_HUMAN)
Sequence A:  QQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSK
RDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFST
VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRG
DVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV
LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP
EPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL
ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNF
YMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSG
WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALG
LPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT
NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARR
QARIDSGSEVIVGVNKYQLEKEDTVEVLAIDNTSVRNRQI
EKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDA
SRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESK
EITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIA
TGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLA
AGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFE
VGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQS
B:  QQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSK
RDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFST
VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRG
DVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV
LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP
EPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL
ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNF
YMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSG
WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALG
LPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT
NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARR
QARIDSGSEVIVGVNKYQLEKEDTVEVLAIDNTSVRNRQI
EKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDA
SRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESK
EITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIA
TGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLA
AGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFE
VGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQ
Description


Functional site

1) chain A
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

2) chain A
residue 138
type
sequence F
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

3) chain A
residue 140
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

4) chain A
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

5) chain A
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

6) chain A
residue 227
type
sequence V
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

7) chain A
residue 228
type
sequence R
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

8) chain A
residue 230
type
sequence T
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

9) chain A
residue 264
type
sequence Y
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

10) chain A
residue 265
type
sequence H
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

11) chain A
residue 268
type
sequence E
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

12) chain A
residue 355
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

13) chain A
residue 356
type
sequence W
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

14) chain A
residue 358
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

15) chain A
residue 392
type
sequence E
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

16) chain A
residue 395
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

17) chain A
residue 396
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

18) chain A
residue 476
type
sequence Q
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

19) chain A
residue 626
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

20) chain A
residue 627
type
sequence H
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

21) chain A
residue 628
type
sequence D
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

22) chain A
residue 629
type
sequence R
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

23) chain A
residue 630
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

24) chain A
residue 634
type
sequence I
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

25) chain A
residue 670
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

26) chain A
residue 672
type
sequence S
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

27) chain A
residue 674
type
sequence L
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

28) chain A
residue 676
type
sequence A
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

29) chain A
residue 702
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

30) chain A
residue 703
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

31) chain A
residue 704
type
sequence V
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

32) chain A
residue 722
type
sequence F
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

33) chain A
residue 723
type
sequence G
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

34) chain A
residue 724
type
sequence P
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

35) chain A
residue 726
type
sequence T
description BINDING SITE FOR RESIDUE B12 A 3001
source : AC1

36) chain A
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

37) chain A
residue 112
type
sequence G
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

38) chain A
residue 137
type
sequence A
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

39) chain A
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

40) chain A
residue 264
type
sequence Y
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

41) chain A
residue 352
type
sequence Q
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

42) chain A
residue 355
type
sequence G
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

43) chain A
residue 388
type
sequence N
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

44) chain A
residue 392
type
sequence E
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

45) chain A
residue 396
type
sequence L
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

46) chain A
residue 397
type
sequence P
description BINDING SITE FOR RESIDUE 5AD A 4001
source : AC2

47) chain A
residue 96
type
sequence Y
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

48) chain A
residue 98
type
sequence T
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

49) chain A
residue 99
type
sequence M
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

50) chain A
residue 103
type
sequence R
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

51) chain A
residue 106
type
sequence T
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

52) chain A
residue 108
type
sequence R
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

53) chain A
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

54) chain A
residue 135
type
sequence S
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

55) chain A
residue 185
type
sequence S
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

56) chain A
residue 187
type
sequence T
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

57) chain A
residue 216
type
sequence T
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

58) chain A
residue 218
type
sequence Q
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

59) chain A
residue 228
type
sequence R
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

60) chain A
residue 255
type
sequence K
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

61) chain A
residue 257
type
sequence N
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

62) chain A
residue 265
type
sequence H
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

63) chain A
residue 304
type
sequence R
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

64) chain A
residue 306
type
sequence S
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

65) chain A
residue 308
type
sequence F
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

66) chain A
residue 348
type
sequence R
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

67) chain A
residue 349
type
sequence A
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

68) chain A
residue 350
type
sequence H
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

69) chain A
residue 352
type
sequence Q
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

70) chain A
residue 383
type
sequence Q
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

71) chain B
residue 50
type
sequence Q
description BINDING SITE FOR RESIDUE MLC A 5001
source : AC3

72) chain B
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

73) chain B
residue 138
type
sequence F
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

74) chain B
residue 140
type
sequence L
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

75) chain B
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

76) chain B
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

77) chain B
residue 227
type
sequence V
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

78) chain B
residue 228
type
sequence R
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

79) chain B
residue 230
type
sequence T
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

80) chain B
residue 264
type
sequence Y
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

81) chain B
residue 268
type
sequence E
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

82) chain B
residue 355
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

83) chain B
residue 356
type
sequence W
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

84) chain B
residue 358
type
sequence L
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

85) chain B
residue 392
type
sequence E
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

86) chain B
residue 395
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

87) chain B
residue 396
type
sequence L
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

88) chain B
residue 476
type
sequence Q
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

89) chain B
residue 626
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

90) chain B
residue 627
type
sequence H
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

91) chain B
residue 628
type
sequence D
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

92) chain B
residue 629
type
sequence R
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

93) chain B
residue 630
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

94) chain B
residue 634
type
sequence I
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

95) chain B
residue 670
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

96) chain B
residue 672
type
sequence S
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

97) chain B
residue 674
type
sequence L
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

98) chain B
residue 676
type
sequence A
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

99) chain B
residue 702
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

100) chain B
residue 703
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

101) chain B
residue 704
type
sequence V
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

102) chain B
residue 722
type
sequence F
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

103) chain B
residue 723
type
sequence G
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

104) chain B
residue 726
type
sequence T
description BINDING SITE FOR RESIDUE B12 B 3001
source : AC4

105) chain B
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

106) chain B
residue 112
type
sequence G
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

107) chain B
residue 137
type
sequence A
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

108) chain B
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

109) chain B
residue 264
type
sequence Y
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

110) chain B
residue 352
type
sequence Q
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

111) chain B
residue 388
type
sequence N
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

112) chain B
residue 392
type
sequence E
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

113) chain B
residue 396
type
sequence L
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

114) chain B
residue 397
type
sequence P
description BINDING SITE FOR RESIDUE 5AD B 4001
source : AC5

115) chain A
residue 50
type
sequence Q
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

116) chain B
residue 96
type
sequence Y
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

117) chain B
residue 98
type
sequence T
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

118) chain B
residue 99
type
sequence M
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

119) chain B
residue 102
type
sequence F
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

120) chain B
residue 103
type
sequence R
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

121) chain B
residue 106
type
sequence T
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

122) chain B
residue 108
type
sequence R
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

123) chain B
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

124) chain B
residue 185
type
sequence S
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

125) chain B
residue 187
type
sequence T
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

126) chain B
residue 216
type
sequence T
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

127) chain B
residue 218
type
sequence Q
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

128) chain B
residue 228
type
sequence R
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

129) chain B
residue 255
type
sequence K
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

130) chain B
residue 257
type
sequence N
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

131) chain B
residue 265
type
sequence H
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

132) chain B
residue 304
type
sequence R
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

133) chain B
residue 306
type
sequence S
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

134) chain B
residue 308
type
sequence F
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

135) chain B
residue 348
type
sequence R
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

136) chain B
residue 349
type
sequence A
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

137) chain B
residue 350
type
sequence H
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

138) chain B
residue 352
type
sequence Q
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

139) chain B
residue 383
type
sequence Q
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

140) chain B
residue 384
type
sequence S
description BINDING SITE FOR RESIDUE MLC B 5001
source : AC6

141) chain A
residue 481
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

142) chain B
residue 481
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

143) chain A
residue 403-428
type prosite
sequence RIARNTQIIIQEESGIPKVADPWGGS
description METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS
source prosite : PS00544

144) chain A
residue 89
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

145) chain A
residue 212
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

146) chain A
residue 335
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

147) chain A
residue 602
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

148) chain B
residue 89
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

149) chain B
residue 212
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

150) chain B
residue 335
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

151) chain B
residue 602
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI3

152) chain A
residue 343
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI4

153) chain A
residue 595
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI4

154) chain B
residue 343
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI4

155) chain B
residue 595
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P16332
source Swiss-Prot : SWS_FT_FI4

156) chain A
residue 50
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

157) chain B
residue 96
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

158) chain B
residue 106
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

159) chain B
residue 216
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

160) chain B
residue 228
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

161) chain B
residue 255
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

162) chain B
residue 265
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

163) chain B
residue 304
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

164) chain A
residue 96
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

165) chain A
residue 106
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

166) chain A
residue 216
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

167) chain A
residue 228
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

168) chain A
residue 255
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

169) chain A
residue 265
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

170) chain A
residue 304
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

171) chain B
residue 50
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI1

172) chain A
residue 627
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI2

173) chain B
residue 627
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:20876572
source Swiss-Prot : SWS_FT_FI2


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