eF-site ID 5zxh-D
PDB Code 5zxh
Chain D

click to enlarge
Title The structure of MT189-tubulin complex
Classification STRUCTURAL PROTEIN
Compound Tubulin alpha-1B chain
Source (E1BQ43_CHICK)
Sequence D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS
DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY
CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT
QQMFDSKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQM
LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN
STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE
AESNMNDLVSEYQQYQDATAD
Description


Functional site

1) chain D
residue 252
type
sequence K
description binding site for residue GTP C 501
source : AD1

2) chain D
residue 10
type
sequence G
description binding site for residue GTP D 501
source : AD4

3) chain D
residue 11
type
sequence Q
description binding site for residue GTP D 501
source : AD4

4) chain D
residue 12
type
sequence C
description binding site for residue GTP D 501
source : AD4

5) chain D
residue 97
type
sequence A
description binding site for residue GTP D 501
source : AD4

6) chain D
residue 98
type
sequence G
description binding site for residue GTP D 501
source : AD4

7) chain D
residue 99
type
sequence N
description binding site for residue GTP D 501
source : AD4

8) chain D
residue 138
type
sequence S
description binding site for residue GTP D 501
source : AD4

9) chain D
residue 141
type
sequence G
description binding site for residue GTP D 501
source : AD4

10) chain D
residue 142
type
sequence G
description binding site for residue GTP D 501
source : AD4

11) chain D
residue 143
type
sequence T
description binding site for residue GTP D 501
source : AD4

12) chain D
residue 144
type
sequence G
description binding site for residue GTP D 501
source : AD4

13) chain D
residue 175
type
sequence V
description binding site for residue GTP D 501
source : AD4

14) chain D
residue 176
type
sequence S
description binding site for residue GTP D 501
source : AD4

15) chain D
residue 181
type
sequence E
description binding site for residue GTP D 501
source : AD4

16) chain D
residue 204
type
sequence N
description binding site for residue GTP D 501
source : AD4

17) chain D
residue 222
type
sequence Y
description binding site for residue GTP D 501
source : AD4

18) chain D
residue 226
type
sequence N
description binding site for residue GTP D 501
source : AD4

19) chain D
residue 236
type
sequence V
description binding site for residue 9LX D 503
source : AD6

20) chain D
residue 239
type
sequence C
description binding site for residue 9LX D 503
source : AD6

21) chain D
residue 240
type
sequence L
description binding site for residue 9LX D 503
source : AD6

22) chain D
residue 246
type
sequence L
description binding site for residue 9LX D 503
source : AD6

23) chain D
residue 249
type
sequence D
description binding site for residue 9LX D 503
source : AD6

24) chain D
residue 252
type
sequence K
description binding site for residue 9LX D 503
source : AD6

25) chain D
residue 253
type
sequence L
description binding site for residue 9LX D 503
source : AD6

26) chain D
residue 256
type
sequence N
description binding site for residue 9LX D 503
source : AD6

27) chain D
residue 313
type
sequence V
description binding site for residue 9LX D 503
source : AD6

28) chain D
residue 316
type
sequence V
description binding site for residue 9LX D 503
source : AD6

29) chain D
residue 350
type
sequence K
description binding site for residue 9LX D 503
source : AD6

30) chain D
residue 351
type
sequence T
description binding site for residue 9LX D 503
source : AD6

31) chain D
residue 352
type
sequence A
description binding site for residue 9LX D 503
source : AD6

32) chain D
residue 142
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

33) chain D
residue 143
type MOD_RES
sequence T
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

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

35) chain D
residue 204
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

36) chain D
residue 226
type MOD_RES
sequence N
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

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

38) chain D
residue 138
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI1

39) chain D
residue 58
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

40) chain D
residue 324
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

41) chain D
residue 285
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI7

42) chain D
residue 290
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI7

43) chain D
residue 318
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
source Swiss-Prot : SWS_FT_FI8

44) chain D
residue 69
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P68363
source Swiss-Prot : SWS_FT_FI2

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

46) chain D
residue 55
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
source Swiss-Prot : SWS_FT_FI4

47) chain D
residue 58
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
source Swiss-Prot : SWS_FT_FI5

48) chain D
residue 172
type MOD_RES
sequence S
description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
source Swiss-Prot : SWS_FT_FI6


Display surface

Download
Links