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

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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 L:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF
NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP
EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC
TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF
SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI
YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN
VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA
EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN
AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA
KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV
GEGMEEGEFSEAREDMAALEKDYEEVGV
Description


Functional site

1) chain L
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

2) chain L
residue 11
type
sequence Q
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

3) chain L
residue 12
type
sequence A
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

4) chain L
residue 15
type
sequence Q
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

5) chain L
residue 99
type
sequence A
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

6) chain L
residue 100
type
sequence A
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

7) chain L
residue 101
type
sequence N
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

8) chain L
residue 140
type
sequence S
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

9) chain L
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

10) chain L
residue 144
type
sequence G
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

11) chain L
residue 145
type
sequence T
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

12) chain L
residue 146
type
sequence G
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

13) chain L
residue 171
type
sequence I
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

14) chain L
residue 179
type
sequence T
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

15) chain L
residue 183
type
sequence E
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

16) chain L
residue 206
type
sequence N
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

17) chain L
residue 224
type
sequence Y
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

18) chain L
residue 228
type
sequence N
description BINDING SITE FOR RESIDUE GTP L 501
source : BC4

19) chain L
residue 71
type
sequence E
description BINDING SITE FOR RESIDUE MG L 502
source : BC5

20) chain L
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

21) chain L
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

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

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

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

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

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

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

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

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

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

31) chain L
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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