eF-site ID 3jat-K
PDB Code 3jat
Chain K

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Title Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin
Classification STRUCTURAL PROTEIN
Compound Tubulin alpha-1B chain
Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa;
Sequence K:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF
NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP
EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC
TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF
SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI
YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN
VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA
EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN
AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA
KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV
GEGMEEGEFSEAREDMAALEKDYEEVGV
Description


Functional site

1) chain K
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

2) chain K
residue 11
type
sequence Q
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

3) chain K
residue 12
type
sequence A
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

4) chain K
residue 15
type
sequence Q
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

5) chain K
residue 99
type
sequence A
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

6) chain K
residue 100
type
sequence A
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

7) chain K
residue 101
type
sequence N
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

8) chain K
residue 140
type
sequence S
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

9) chain K
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

10) chain K
residue 144
type
sequence G
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

11) chain K
residue 145
type
sequence T
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

12) chain K
residue 146
type
sequence G
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

13) chain K
residue 171
type
sequence I
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

14) chain K
residue 179
type
sequence T
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

15) chain K
residue 183
type
sequence E
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

16) chain K
residue 206
type
sequence N
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

17) chain K
residue 224
type
sequence Y
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

18) chain K
residue 228
type
sequence N
description BINDING SITE FOR RESIDUE GTP K 501
source : CC3

19) chain K
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

20) chain K
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

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

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

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

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

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

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

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

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

29) chain K
residue 48
type MOD_RES
sequence S
description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
source Swiss-Prot : SWS_FT_FI5

30) chain K
residue 232
type MOD_RES
sequence S
description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
source Swiss-Prot : SWS_FT_FI5


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