eF-site ID 6i5c-C
PDB Code 6i5c
Chain C

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Title Long wavelength native-SAD phasing of Tubulin-Stathmin-TTL complex
Classification STRUCTURAL PROTEIN
Compound Tubulin alpha-1B chain
Source (E1BQ43_CHICK)
Sequence C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK
TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK
AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
Description (1)  Tubulin alpha-1B chain, Tubulin beta-2B chain, Stathmin-4, TUBULIN-TYROSINE LIGASE


Functional site

1) chain C
residue 284
type
sequence E
description binding site for residue CA B 502
source : AC6

2) chain C
residue 10
type
sequence G
description binding site for residue GTP C 501
source : AD1

3) chain C
residue 11
type
sequence Q
description binding site for residue GTP C 501
source : AD1

4) chain C
residue 12
type
sequence A
description binding site for residue GTP C 501
source : AD1

5) chain C
residue 15
type
sequence Q
description binding site for residue GTP C 501
source : AD1

6) chain C
residue 98
type
sequence D
description binding site for residue GTP C 501
source : AD1

7) chain C
residue 99
type
sequence A
description binding site for residue GTP C 501
source : AD1

8) chain C
residue 100
type
sequence A
description binding site for residue GTP C 501
source : AD1

9) chain C
residue 101
type
sequence N
description binding site for residue GTP C 501
source : AD1

10) chain C
residue 140
type
sequence S
description binding site for residue GTP C 501
source : AD1

11) chain C
residue 143
type
sequence G
description binding site for residue GTP C 501
source : AD1

12) chain C
residue 144
type
sequence G
description binding site for residue GTP C 501
source : AD1

13) chain C
residue 145
type
sequence T
description binding site for residue GTP C 501
source : AD1

14) chain C
residue 146
type
sequence G
description binding site for residue GTP C 501
source : AD1

15) chain C
residue 171
type
sequence I
description binding site for residue GTP C 501
source : AD1

16) chain C
residue 177
type
sequence V
description binding site for residue GTP C 501
source : AD1

17) chain C
residue 179
type
sequence T
description binding site for residue GTP C 501
source : AD1

18) chain C
residue 183
type
sequence E
description binding site for residue GTP C 501
source : AD1

19) chain C
residue 206
type
sequence N
description binding site for residue GTP C 501
source : AD1

20) chain C
residue 224
type
sequence Y
description binding site for residue GTP C 501
source : AD1

21) chain C
residue 228
type
sequence N
description binding site for residue GTP C 501
source : AD1

22) chain C
residue 231
type
sequence I
description binding site for residue GTP C 501
source : AD1

23) chain C
residue 11
type
sequence Q
description binding site for residue MG C 502
source : AD2

24) chain C
residue 69
type
sequence D
description binding site for residue MG C 502
source : AD2

25) chain C
residue 71
type
sequence E
description binding site for residue MG C 502
source : AD2

26) chain C
residue 39
type
sequence D
description binding site for residue CA C 503
source : AD3

27) chain C
residue 41
type
sequence T
description binding site for residue CA C 503
source : AD3

28) chain C
residue 44
type
sequence G
description binding site for residue CA C 503
source : AD3

29) chain C
residue 55
type
sequence E
description binding site for residue CA C 503
source : AD3

30) chain C
residue 233
type
sequence Q
description binding site for residue CL C 504
source : AD4

31) chain C
residue 362
type
sequence V
description binding site for residue CL C 504
source : AD4

32) chain C
residue 363
type
sequence V
description binding site for residue CL C 504
source : AD4

33) chain C
residue 71
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

34) chain C
residue 140
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

35) chain C
residue 144
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

36) chain C
residue 145
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

37) chain C
residue 179
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

38) chain C
residue 206
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

39) chain C
residue 228
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

40) chain C
residue 11
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

41) chain C
residue 48
type MOD_RES
sequence S
description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
source Swiss-Prot : SWS_FT_FI4

42) chain C
residue 232
type MOD_RES
sequence S
description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
source Swiss-Prot : SWS_FT_FI4

43) chain C
residue 370
type MOD_RES
sequence K
description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI8

44) chain C
residue 326
type MOD_RES
sequence K
description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI8


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