eF-site ID 5lov-C
PDB Code 5lov
Chain C

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Title DZ-2384 tubulin complex
Classification CELL CYCLE
Compound Tubulin alpha-1B chain
Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK
TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK
AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRFVDWCPTGFKVGINYQPPTVV
PGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRA
FVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
Description


Functional site

1) chain C
residue 254
type
sequence E
description binding site for residue MG B 503
source : AC6

2) chain C
residue 10
type
sequence G
description binding site for residue GTP C 501
source : AC7

3) chain C
residue 11
type
sequence Q
description binding site for residue GTP C 501
source : AC7

4) chain C
residue 12
type
sequence A
description binding site for residue GTP C 501
source : AC7

5) chain C
residue 15
type
sequence Q
description binding site for residue GTP C 501
source : AC7

6) chain C
residue 16
type
sequence I
description binding site for residue GTP C 501
source : AC7

7) chain C
residue 98
type
sequence D
description binding site for residue GTP C 501
source : AC7

8) chain C
residue 99
type
sequence A
description binding site for residue GTP C 501
source : AC7

9) chain C
residue 100
type
sequence A
description binding site for residue GTP C 501
source : AC7

10) chain C
residue 101
type
sequence N
description binding site for residue GTP C 501
source : AC7

11) chain C
residue 140
type
sequence S
description binding site for residue GTP C 501
source : AC7

12) chain C
residue 143
type
sequence G
description binding site for residue GTP C 501
source : AC7

13) chain C
residue 144
type
sequence G
description binding site for residue GTP C 501
source : AC7

14) chain C
residue 145
type
sequence T
description binding site for residue GTP C 501
source : AC7

15) chain C
residue 146
type
sequence G
description binding site for residue GTP C 501
source : AC7

16) chain C
residue 171
type
sequence I
description binding site for residue GTP C 501
source : AC7

17) chain C
residue 177
type
sequence V
description binding site for residue GTP C 501
source : AC7

18) chain C
residue 179
type
sequence T
description binding site for residue GTP C 501
source : AC7

19) chain C
residue 183
type
sequence E
description binding site for residue GTP C 501
source : AC7

20) chain C
residue 206
type
sequence N
description binding site for residue GTP C 501
source : AC7

21) chain C
residue 224
type
sequence Y
description binding site for residue GTP C 501
source : AC7

22) chain C
residue 228
type
sequence N
description binding site for residue GTP C 501
source : AC7

23) chain C
residue 231
type
sequence I
description binding site for residue GTP C 501
source : AC7

24) chain C
residue 69
type
sequence D
description binding site for residue MG C 502
source : AC8

25) chain C
residue 325
type
sequence P
description binding site for residue 71E C 503
source : AC9

26) chain C
residue 328
type
sequence V
description binding site for residue 71E C 503
source : AC9

27) chain C
residue 329
type
sequence N
description binding site for residue 71E C 503
source : AC9

28) chain C
residue 332
type
sequence I
description binding site for residue 71E C 503
source : AC9

29) chain C
residue 336
type
sequence K
description binding site for residue 71E C 503
source : AC9

30) chain C
residue 351
type
sequence F
description binding site for residue 71E C 503
source : AC9

31) chain C
residue 353
type
sequence V
description binding site for residue 71E C 503
source : AC9

32) chain C
residue 355
type
sequence I
description binding site for residue 71E C 503
source : AC9

33) 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

34) 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

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

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

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

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

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

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

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

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

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

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


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