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

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Title Tubulin-GDP.BeF complex
Classification CELL CYCLE
Compound Tubulin alpha-1B chain
Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK
TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK
AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
Description


Functional site

1) chain C
residue 279
type
sequence E
description binding site for residue CA B 503
source : AC6

2) chain C
residue 10
type
sequence G
description binding site for residue GTP C 501
source : AC9

3) chain C
residue 11
type
sequence Q
description binding site for residue GTP C 501
source : AC9

4) chain C
residue 12
type
sequence A
description binding site for residue GTP C 501
source : AC9

5) chain C
residue 15
type
sequence Q
description binding site for residue GTP C 501
source : AC9

6) chain C
residue 69
type
sequence D
description binding site for residue GTP C 501
source : AC9

7) chain C
residue 98
type
sequence D
description binding site for residue GTP C 501
source : AC9

8) chain C
residue 99
type
sequence A
description binding site for residue GTP C 501
source : AC9

9) chain C
residue 100
type
sequence A
description binding site for residue GTP C 501
source : AC9

10) chain C
residue 101
type
sequence N
description binding site for residue GTP C 501
source : AC9

11) chain C
residue 140
type
sequence S
description binding site for residue GTP C 501
source : AC9

12) chain C
residue 143
type
sequence G
description binding site for residue GTP C 501
source : AC9

13) chain C
residue 144
type
sequence G
description binding site for residue GTP C 501
source : AC9

14) chain C
residue 145
type
sequence T
description binding site for residue GTP C 501
source : AC9

15) chain C
residue 146
type
sequence G
description binding site for residue GTP C 501
source : AC9

16) chain C
residue 171
type
sequence I
description binding site for residue GTP C 501
source : AC9

17) chain C
residue 177
type
sequence V
description binding site for residue GTP C 501
source : AC9

18) chain C
residue 183
type
sequence E
description binding site for residue GTP C 501
source : AC9

19) chain C
residue 206
type
sequence N
description binding site for residue GTP C 501
source : AC9

20) chain C
residue 224
type
sequence Y
description binding site for residue GTP C 501
source : AC9

21) chain C
residue 228
type
sequence N
description binding site for residue GTP C 501
source : AC9

22) chain C
residue 231
type
sequence I
description binding site for residue GTP C 501
source : AC9

23) chain C
residue 39
type
sequence D
description binding site for residue CA C 503
source : AD2

24) chain C
residue 41
type
sequence T
description binding site for residue CA C 503
source : AD2

25) chain C
residue 44
type
sequence G
description binding site for residue CA C 503
source : AD2

26) chain C
residue 55
type
sequence E
description binding site for residue CA C 503
source : AD2

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

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

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

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

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

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

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

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

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

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

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

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


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