eF-site ID 5xag-A
PDB Code 5xag
Chain A

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Title Crystal structure of tubulin-stathmin-TTL-Compound Z2 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
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDS
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 177
type
sequence V
description binding site for residue GTP A 501
source : AC1

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

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

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

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

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

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

20) chain A
residue 11
type
sequence Q
description binding site for residue MG A 502
source : AC2

21) chain A
residue 69
type
sequence D
description binding site for residue MG A 502
source : AC2

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

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

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

25) chain A
residue 275
type
sequence V
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 310
type
sequence G
description binding site for residue GOL A 504
source : AC4

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

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

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

32) chain A
residue 433
type
sequence E
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 158
type
sequence S
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 197
type
sequence H
description binding site for residue GOL A 506
source : AC6

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

42) chain A
residue 179
type
sequence T
description binding site for residue 93X B 508
source : AD5

43) chain A
residue 180
type
sequence A
description binding site for residue 93X B 508
source : AD5

44) chain A
residue 181
type
sequence V
description binding site for residue 93X B 508
source : AD5

45) 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

46) 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

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

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

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

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

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

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

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


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