eF-site ID 5xaf-ABCDEF
PDB Code 5xaf
Chain A, B, C, D, E, F

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Title Crystal structure of tubulin-stathmin-TTL-Compound Z1 complex
Classification STRUCTURAL PROTEIN
Compound Tubulin alpha-1B chain
Source Bos taurus (Bovine) (E1BQ43_CHICK)
Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK
TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK
AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVD
B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS
DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY
CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLQYRALTV
PELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEV
DEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSAT
FIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEM
EFTEAESNMNDLVSEYQQYQDA
C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK
TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK
AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS
DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY
CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT
QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM
LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN
STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE
AESNMNDLVSEYQQYQDATAD
E:  MEVIELNKCTSGQSFEVILKPPSDPSLEEIQKKLEAAEER
RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK
LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK
E
F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM
LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSCTWFPESYVIYPTDEREVFLAAYNGNVWIAKS
ISSEASELLDFIHVIQKYLEKPLLLEPGHRKFDIRSWVLV
DHLYNIYLYREGVLRTSSEPYNSADKTCHLTNHCIQKEYS
NYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHII
RSCLMCIEPAISTKHLHYQSFQLFGFDFMVDEELKVWLIE
VNGAPACAQKLYAELCQGIVDVAISSVFPLASIFIKL
Description


Functional site

1) chain A
residue 10
type
sequence G
description binding site for residue GTP A 501
source : AC1

2) chain A
residue 11
type
sequence Q
description binding site for residue GTP A 501
source : AC1

3) chain A
residue 12
type
sequence A
description binding site for residue GTP A 501
source : AC1

4) chain A
residue 15
type
sequence Q
description binding site for residue GTP A 501
source : AC1

5) chain A
residue 98
type
sequence D
description binding site for residue GTP A 501
source : AC1

6) chain A
residue 99
type
sequence A
description binding site for residue GTP A 501
source : AC1

7) chain A
residue 101
type
sequence N
description binding site for residue GTP A 501
source : AC1

8) chain A
residue 140
type
sequence S
description binding site for residue GTP A 501
source : AC1

9) chain A
residue 143
type
sequence G
description binding site for residue GTP A 501
source : AC1

10) chain A
residue 144
type
sequence G
description binding site for residue GTP A 501
source : AC1

11) chain A
residue 145
type
sequence T
description binding site for residue GTP A 501
source : AC1

12) chain A
residue 146
type
sequence G
description binding site for residue GTP A 501
source : AC1

13) chain A
residue 171
type
sequence I
description binding site for residue GTP A 501
source : AC1

14) chain A
residue 177
type
sequence V
description binding site for residue GTP A 501
source : AC1

15) chain A
residue 179
type
sequence T
description binding site for residue GTP A 501
source : AC1

16) chain A
residue 183
type
sequence E
description binding site for residue GTP A 501
source : AC1

17) chain A
residue 206
type
sequence N
description binding site for residue GTP A 501
source : AC1

18) chain A
residue 224
type
sequence Y
description binding site for residue GTP A 501
source : AC1

19) chain A
residue 228
type
sequence N
description binding site for residue GTP A 501
source : AC1

20) chain A
residue 231
type
sequence I
description binding site for residue GTP A 501
source : AC1

21) chain A
residue 71
type
sequence E
description binding site for residue MG A 502
source : AC2

22) chain A
residue 216
type
sequence N
description binding site for residue GOL A 503
source : AC3

23) chain A
residue 274
type
sequence P
description binding site for residue GOL A 503
source : AC3

24) chain A
residue 275
type
sequence V
description binding site for residue GOL A 503
source : AC3

25) chain A
residue 294
type
sequence A
description binding site for residue GOL A 503
source : AC3

26) chain A
residue 300
type
sequence N
description binding site for residue GOL A 503
source : AC3

27) chain A
residue 309
type
sequence H
description binding site for residue GOL A 504
source : AC4

28) chain A
residue 382
type
sequence T
description binding site for residue GOL A 504
source : AC4

29) chain A
residue 383
type
sequence A
description binding site for residue GOL A 504
source : AC4

30) chain A
residue 386
type
sequence E
description binding site for residue GOL A 504
source : AC4

31) chain A
residue 433
type
sequence E
description binding site for residue GOL A 504
source : AC4

32) chain F
residue 66
type
sequence R
description binding site for residue GOL A 504
source : AC4

33) chain A
residue 39
type
sequence D
description binding site for residue CA A 505
source : AC5

34) chain A
residue 41
type
sequence T
description binding site for residue CA A 505
source : AC5

35) chain A
residue 44
type
sequence G
description binding site for residue CA A 505
source : AC5

36) chain A
residue 55
type
sequence E
description binding site for residue CA A 505
source : AC5

37) chain A
residue 162
type
sequence G
description binding site for residue GOL A 506
source : AC6

38) chain A
residue 164
type
sequence K
description binding site for residue GOL A 506
source : AC6

39) chain A
residue 166
type
sequence K
description binding site for residue GOL A 506
source : AC6

40) chain A
residue 196
type
sequence E
description binding site for residue GOL A 506
source : AC6

41) chain A
residue 197
type
sequence H
description binding site for residue GOL A 506
source : AC6

42) chain A
residue 199
type
sequence D
description binding site for residue GOL A 506
source : AC6

43) chain E
residue 44
type
sequence D
description binding site for residue GOL A 506
source : AC6

44) chain B
residue 10
type
sequence G
description binding site for residue GDP B 501
source : AC7

45) chain B
residue 11
type
sequence Q
description binding site for residue GDP B 501
source : AC7

46) chain B
residue 12
type
sequence C
description binding site for residue GDP B 501
source : AC7

47) chain B
residue 15
type
sequence Q
description binding site for residue GDP B 501
source : AC7

48) chain B
residue 140
type
sequence S
description binding site for residue GDP B 501
source : AC7

49) chain B
residue 143
type
sequence G
description binding site for residue GDP B 501
source : AC7

50) chain B
residue 144
type
sequence G
description binding site for residue GDP B 501
source : AC7

51) chain B
residue 145
type
sequence T
description binding site for residue GDP B 501
source : AC7

52) chain B
residue 146
type
sequence G
description binding site for residue GDP B 501
source : AC7

53) chain B
residue 177
type
sequence V
description binding site for residue GDP B 501
source : AC7

54) chain B
residue 179
type
sequence D
description binding site for residue GDP B 501
source : AC7

55) chain B
residue 183
type
sequence E
description binding site for residue GDP B 501
source : AC7

56) chain B
residue 206
type
sequence N
description binding site for residue GDP B 501
source : AC7

57) chain B
residue 224
type
sequence Y
description binding site for residue GDP B 501
source : AC7

58) chain B
residue 228
type
sequence N
description binding site for residue GDP B 501
source : AC7

59) chain B
residue 11
type
sequence Q
description binding site for residue MG B 502
source : AC8

60) chain B
residue 179
type
sequence D
description binding site for residue MG B 502
source : AC8

61) chain B
residue 401
type
sequence R
description binding site for residue GOL B 503
source : AC9

62) chain C
residue 262
type
sequence Y
description binding site for residue GOL B 503
source : AC9

63) chain C
residue 434
type
sequence E
description binding site for residue GOL B 503
source : AC9

64) chain C
residue 435
type
sequence V
description binding site for residue GOL B 503
source : AC9

65) chain B
residue 177
type
sequence V
description binding site for residue GOL B 504
source : AD1

66) chain B
residue 178
type
sequence S
description binding site for residue GOL B 504
source : AD1

67) chain B
residue 222
type
sequence P
description binding site for residue GOL B 504
source : AD1

68) chain B
residue 224
type
sequence Y
description binding site for residue GOL B 504
source : AD1

69) chain B
residue 233
type
sequence A
description binding site for residue GOL B 505
source : AD2

70) chain B
residue 236
type
sequence S
description binding site for residue GOL B 505
source : AD2

71) chain B
residue 237
type
sequence G
description binding site for residue GOL B 505
source : AD2

72) chain B
residue 272
type
sequence F
description binding site for residue GOL B 505
source : AD2

73) chain B
residue 320
type
sequence R
description binding site for residue GOL B 505
source : AD2

74) chain B
residue 360
type
sequence P
description binding site for residue GOL B 505
source : AD2

75) chain B
residue 374
type
sequence S
description binding site for residue GOL B 505
source : AD2

76) chain B
residue 375
type
sequence A
description binding site for residue GOL B 505
source : AD2

77) chain B
residue 376
type
sequence T
description binding site for residue GOL B 505
source : AD2

78) chain B
residue 110
type
sequence E
description binding site for residue CA B 506
source : AD3

79) chain B
residue 113
type
sequence E
description binding site for residue CA B 506
source : AD3

80) chain B
residue 158
type
sequence R
description binding site for residue MES B 507
source : AD4

81) chain B
residue 162
type
sequence P
description binding site for residue MES B 507
source : AD4

82) chain B
residue 163
type
sequence D
description binding site for residue MES B 507
source : AD4

83) chain B
residue 164
type
sequence R
description binding site for residue MES B 507
source : AD4

84) chain B
residue 166
type
sequence M
description binding site for residue MES B 507
source : AD4

85) chain B
residue 197
type
sequence N
description binding site for residue MES B 507
source : AD4

86) chain B
residue 199
type
sequence D
description binding site for residue MES B 507
source : AD4

87) chain B
residue 253
type
sequence R
description binding site for residue MES B 507
source : AD4

88) chain A
residue 179
type
sequence T
description binding site for residue 84F B 508
source : AD5

89) chain A
residue 180
type
sequence A
description binding site for residue 84F B 508
source : AD5

90) chain A
residue 181
type
sequence V
description binding site for residue 84F B 508
source : AD5

91) chain B
residue 237
type
sequence G
description binding site for residue 84F B 508
source : AD5

92) chain B
residue 238
type
sequence V
description binding site for residue 84F B 508
source : AD5

93) chain B
residue 241
type
sequence C
description binding site for residue 84F B 508
source : AD5

94) chain B
residue 242
type
sequence L
description binding site for residue 84F B 508
source : AD5

95) chain B
residue 250
type
sequence A
description binding site for residue 84F B 508
source : AD5

96) chain B
residue 251
type
sequence D
description binding site for residue 84F B 508
source : AD5

97) chain B
residue 255
type
sequence L
description binding site for residue 84F B 508
source : AD5

98) chain B
residue 258
type
sequence N
description binding site for residue 84F B 508
source : AD5

99) chain B
residue 315
type
sequence V
description binding site for residue 84F B 508
source : AD5

100) chain B
residue 316
type
sequence A
description binding site for residue 84F B 508
source : AD5

101) chain B
residue 317
type
sequence A
description binding site for residue 84F B 508
source : AD5

102) chain B
residue 318
type
sequence I
description binding site for residue 84F B 508
source : AD5

103) chain B
residue 350
type
sequence N
description binding site for residue 84F B 508
source : AD5

104) chain B
residue 352
type
sequence K
description binding site for residue 84F B 508
source : AD5

105) chain B
residue 100
type
sequence G
description binding site for residue GOL C 501
source : AD6

106) chain B
residue 105
type
sequence K
description binding site for residue GOL C 501
source : AD6

107) chain C
residue 253
type
sequence T
description binding site for residue GOL C 501
source : AD6

108) chain C
residue 257
type
sequence T
description binding site for residue GOL C 501
source : AD6

109) chain C
residue 10
type
sequence G
description binding site for residue GTP C 502
source : AD7

110) chain C
residue 11
type
sequence Q
description binding site for residue GTP C 502
source : AD7

111) chain C
residue 12
type
sequence A
description binding site for residue GTP C 502
source : AD7

112) chain C
residue 15
type
sequence Q
description binding site for residue GTP C 502
source : AD7

113) chain C
residue 98
type
sequence D
description binding site for residue GTP C 502
source : AD7

114) chain C
residue 99
type
sequence A
description binding site for residue GTP C 502
source : AD7

115) chain C
residue 101
type
sequence N
description binding site for residue GTP C 502
source : AD7

116) chain C
residue 140
type
sequence S
description binding site for residue GTP C 502
source : AD7

117) chain C
residue 143
type
sequence G
description binding site for residue GTP C 502
source : AD7

118) chain C
residue 144
type
sequence G
description binding site for residue GTP C 502
source : AD7

119) chain C
residue 145
type
sequence T
description binding site for residue GTP C 502
source : AD7

120) chain C
residue 146
type
sequence G
description binding site for residue GTP C 502
source : AD7

121) chain C
residue 177
type
sequence V
description binding site for residue GTP C 502
source : AD7

122) chain C
residue 179
type
sequence T
description binding site for residue GTP C 502
source : AD7

123) chain C
residue 183
type
sequence E
description binding site for residue GTP C 502
source : AD7

124) chain C
residue 206
type
sequence N
description binding site for residue GTP C 502
source : AD7

125) chain C
residue 224
type
sequence Y
description binding site for residue GTP C 502
source : AD7

126) chain C
residue 228
type
sequence N
description binding site for residue GTP C 502
source : AD7

127) chain C
residue 98
type
sequence D
description binding site for residue MG C 503
source : AD8

128) chain C
residue 221
type
sequence R
description binding site for residue GOL C 504
source : AD9

129) chain C
residue 222
type
sequence P
description binding site for residue GOL C 504
source : AD9

130) chain C
residue 224
type
sequence Y
description binding site for residue GOL C 504
source : AD9

131) chain D
residue 247
type
sequence Q
description binding site for residue GOL C 504
source : AD9

132) chain C
residue 288
type
sequence V
description binding site for residue GOL C 505
source : AE1

133) chain C
residue 322
type
sequence D
description binding site for residue GOL C 505
source : AE1

134) chain C
residue 327
type
sequence D
description binding site for residue GOL C 505
source : AE1

135) chain C
residue 373
type
sequence R
description binding site for residue GOL C 505
source : AE1

136) chain C
residue 163
type
sequence K
description binding site for residue GOL C 506
source : AE2

137) chain C
residue 164
type
sequence K
description binding site for residue GOL C 506
source : AE2

138) chain C
residue 166
type
sequence K
description binding site for residue GOL C 506
source : AE2

139) chain C
residue 196
type
sequence E
description binding site for residue GOL C 506
source : AE2

140) chain C
residue 197
type
sequence H
description binding site for residue GOL C 506
source : AE2

141) chain C
residue 199
type
sequence D
description binding site for residue GOL C 506
source : AE2

142) chain E
residue 93
type
sequence F
description binding site for residue GOL C 506
source : AE2

143) chain B
residue 113
type
sequence E
description binding site for residue CA C 507
source : AE3

144) chain C
residue 282
type
sequence Y
description binding site for residue CA C 507
source : AE3

145) chain C
residue 262
type
sequence Y
description binding site for residue IMD C 508
source : AE4

146) chain C
residue 431
type
sequence D
description binding site for residue IMD C 508
source : AE4

147) chain C
residue 4
type
sequence C
description binding site for residue IMD C 509
source : AE5

148) chain C
residue 133
type
sequence Q
description binding site for residue IMD C 509
source : AE5

149) chain C
residue 165
type
sequence S
description binding site for residue IMD C 509
source : AE5

150) chain C
residue 167
type
sequence L
description binding site for residue IMD C 509
source : AE5

151) chain C
residue 253
type
sequence T
description binding site for residue IMD C 509
source : AE5

152) chain C
residue 256
type
sequence Q
description binding site for residue IMD C 509
source : AE5

153) chain D
residue 10
type
sequence G
description binding site for residue GDP D 501
source : AE6

154) chain D
residue 11
type
sequence Q
description binding site for residue GDP D 501
source : AE6

155) chain D
residue 12
type
sequence C
description binding site for residue GDP D 501
source : AE6

156) chain D
residue 15
type
sequence Q
description binding site for residue GDP D 501
source : AE6

157) chain D
residue 99
type
sequence A
description binding site for residue GDP D 501
source : AE6

158) chain D
residue 140
type
sequence S
description binding site for residue GDP D 501
source : AE6

159) chain D
residue 143
type
sequence G
description binding site for residue GDP D 501
source : AE6

160) chain D
residue 144
type
sequence G
description binding site for residue GDP D 501
source : AE6

161) chain D
residue 145
type
sequence T
description binding site for residue GDP D 501
source : AE6

162) chain D
residue 146
type
sequence G
description binding site for residue GDP D 501
source : AE6

163) chain D
residue 177
type
sequence V
description binding site for residue GDP D 501
source : AE6

164) chain D
residue 183
type
sequence E
description binding site for residue GDP D 501
source : AE6

165) chain D
residue 206
type
sequence N
description binding site for residue GDP D 501
source : AE6

166) chain D
residue 224
type
sequence Y
description binding site for residue GDP D 501
source : AE6

167) chain D
residue 228
type
sequence N
description binding site for residue GDP D 501
source : AE6

168) chain D
residue 11
type
sequence Q
description binding site for residue MG D 502
source : AE7

169) chain D
residue 101
type
sequence N
description binding site for residue MG D 502
source : AE7

170) chain D
residue 177
type
sequence V
description binding site for residue GOL D 503
source : AE8

171) chain D
residue 222
type
sequence P
description binding site for residue GOL D 503
source : AE8

172) chain D
residue 223
type
sequence T
description binding site for residue GOL D 503
source : AE8

173) chain D
residue 224
type
sequence Y
description binding site for residue GOL D 503
source : AE8

174) chain C
residue 179
type
sequence T
description binding site for residue 84F D 505
source : AE9

175) chain C
residue 180
type
sequence A
description binding site for residue 84F D 505
source : AE9

176) chain C
residue 181
type
sequence V
description binding site for residue 84F D 505
source : AE9

177) chain D
residue 237
type
sequence G
description binding site for residue 84F D 505
source : AE9

178) chain D
residue 238
type
sequence V
description binding site for residue 84F D 505
source : AE9

179) chain D
residue 241
type
sequence C
description binding site for residue 84F D 505
source : AE9

180) chain D
residue 250
type
sequence A
description binding site for residue 84F D 505
source : AE9

181) chain D
residue 251
type
sequence D
description binding site for residue 84F D 505
source : AE9

182) chain D
residue 254
type
sequence K
description binding site for residue 84F D 505
source : AE9

183) chain D
residue 255
type
sequence L
description binding site for residue 84F D 505
source : AE9

184) chain D
residue 258
type
sequence N
description binding site for residue 84F D 505
source : AE9

185) chain D
residue 259
type
sequence M
description binding site for residue 84F D 505
source : AE9

186) chain D
residue 317
type
sequence A
description binding site for residue 84F D 505
source : AE9

187) chain D
residue 318
type
sequence I
description binding site for residue 84F D 505
source : AE9

188) chain D
residue 352
type
sequence K
description binding site for residue 84F D 505
source : AE9

189) chain D
residue 354
type
sequence A
description binding site for residue 84F D 505
source : AE9

190) chain D
residue 378
type
sequence I
description binding site for residue 84F D 505
source : AE9

191) chain F
residue 200
type
sequence D
description binding site for residue MG F 401
source : AF1

192) chain F
residue 222
type
sequence R
description binding site for residue MG F 401
source : AF1

193) chain F
residue 242
type
sequence N
description binding site for residue MG F 401
source : AF1

194) chain F
residue 318
type
sequence D
description binding site for residue MG F 401
source : AF1

195) chain F
residue 74
type
sequence K
description binding site for residue ACP F 402
source : AF2

196) chain F
residue 95
type
sequence P
description binding site for residue ACP F 402
source : AF2

197) chain F
residue 183
type
sequence Q
description binding site for residue ACP F 402
source : AF2

198) chain F
residue 184
type
sequence K
description binding site for residue ACP F 402
source : AF2

199) chain F
residue 186
type
sequence L
description binding site for residue ACP F 402
source : AF2

200) chain F
residue 198
type
sequence K
description binding site for residue ACP F 402
source : AF2

201) chain F
residue 239
type
sequence H
description binding site for residue ACP F 402
source : AF2

202) chain F
residue 240
type
sequence L
description binding site for residue ACP F 402
source : AF2

203) chain F
residue 241
type
sequence T
description binding site for residue ACP F 402
source : AF2

204) chain F
residue 330
type
sequence I
description binding site for residue ACP F 402
source : AF2

205) chain F
residue 331
type
sequence E
description binding site for residue ACP F 402
source : AF2

206) chain C
residue 407
type
sequence W
description binding site for residues GOL D 504 and IMD E 201
source : AF3

207) chain C
residue 410
type
sequence G
description binding site for residues GOL D 504 and IMD E 201
source : AF3

208) chain C
residue 411
type
sequence E
description binding site for residues GOL D 504 and IMD E 201
source : AF3

209) chain D
residue 162
type
sequence P
description binding site for residues GOL D 504 and IMD E 201
source : AF3

210) chain D
residue 164
type
sequence R
description binding site for residues GOL D 504 and IMD E 201
source : AF3

211) chain D
residue 168
type
sequence T
description binding site for residues GOL D 504 and IMD E 201
source : AF3

212) chain D
residue 170
type
sequence S
description binding site for residues GOL D 504 and IMD E 201
source : AF3

213) chain D
residue 198
type
sequence T
description binding site for residues GOL D 504 and IMD E 201
source : AF3

214) chain D
residue 199
type
sequence D
description binding site for residues GOL D 504 and IMD E 201
source : AF3

215) chain D
residue 200
type
sequence E
description binding site for residues GOL D 504 and IMD E 201
source : AF3

216) chain D
residue 202
type
sequence Y
description binding site for residues GOL D 504 and IMD E 201
source : AF3

217) chain D
residue 203
type
sequence C
description binding site for residues GOL D 504 and IMD E 201
source : AF3

218) chain D
residue 253
type
sequence R
description binding site for residues GOL D 504 and IMD E 201
source : AF3

219) chain D
residue 266
type
sequence H
description binding site for residues GOL D 504 and IMD E 201
source : AF3

220) chain D
residue 267
type
sequence F
description binding site for residues GOL D 504 and IMD E 201
source : AF3

221) chain D
residue 268
type
sequence F
description binding site for residues GOL D 504 and IMD E 201
source : AF3

222) chain E
residue 112
type
sequence R
description binding site for residues GOL D 504 and IMD E 201
source : AF3

223) chain B
residue 142-148
type prosite
sequence GGGTGSG
description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
source prosite : PS00227

224) chain A
residue 142-148
type prosite
sequence GGGTGSG
description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
source prosite : PS00227

225) chain B
residue 1-4
type prosite
sequence MREI
description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
source prosite : PS00228

226) chain E
residue 73-82
type prosite
sequence AEKREHEREV
description STATHMIN_2 Stathmin family signature 2. AEKREHEREV
source prosite : PS01041

227) chain E
residue 46
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

228) chain D
residue 144
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

229) chain D
residue 145
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

230) chain D
residue 146
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

231) chain D
residue 206
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

232) chain D
residue 228
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

233) chain B
residue 140
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

234) chain B
residue 144
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

235) chain B
residue 145
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

236) chain B
residue 146
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

237) chain B
residue 206
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

238) chain B
residue 228
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

239) chain D
residue 11
type MOD_RES
sequence Q
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

240) chain D
residue 140
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

241) chain B
residue 60
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI10

242) chain D
residue 60
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI10

243) chain B
residue 326
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI11

244) chain D
residue 326
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI11

245) chain A
residue 326
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI12

246) chain A
residue 370
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI12

247) chain C
residue 326
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI12

248) chain C
residue 370
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI12

249) chain C
residue 71
type LIPID
sequence E
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

250) chain C
residue 140
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

251) chain C
residue 144
type LIPID
sequence G
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

252) chain C
residue 145
type LIPID
sequence T
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

253) chain C
residue 179
type LIPID
sequence T
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

254) chain C
residue 206
type LIPID
sequence N
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

255) chain C
residue 228
type LIPID
sequence N
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

256) chain A
residue 140
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

257) chain A
residue 144
type LIPID
sequence G
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

258) chain A
residue 145
type LIPID
sequence T
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

259) chain A
residue 179
type LIPID
sequence T
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

260) chain A
residue 206
type LIPID
sequence N
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

261) chain A
residue 228
type LIPID
sequence N
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

262) chain C
residue 11
type LIPID
sequence Q
description S-palmitoyl cysteine => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

263) chain B
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI3

264) chain D
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI3

265) chain B
residue 57
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
source Swiss-Prot : SWS_FT_FI4

266) chain D
residue 57
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
source Swiss-Prot : SWS_FT_FI4

267) chain B
residue 60
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI5

268) chain D
residue 60
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI5

269) chain C
residue 48
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI5

270) chain C
residue 232
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI5

271) chain B
residue 174
type MOD_RES
sequence S
description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
source Swiss-Prot : SWS_FT_FI6

272) chain D
residue 174
type MOD_RES
sequence S
description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
source Swiss-Prot : SWS_FT_FI6

273) chain B
residue 287
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI7

274) chain B
residue 292
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI7

275) chain D
residue 287
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI7

276) chain D
residue 292
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI7

277) chain B
residue 320
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI8

278) chain D
residue 320
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI8


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