eF-site ID 1dej-AS
PDB Code 1dej
Chain A, S

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Title CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 1
Classification CONTRACTILE PROTEIN
Compound GELSOLIN
Source (ACT8_DICDI)
Sequence A:  DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRH
TGKDSYVGDEAQSKRGILTLKYPIEXGIVTNWDDMEKIWH
HTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETF
NTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYE
GYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAERE
IVRDIKEKLAYVALDFEAEMKAYKESSALEKSYELPDGQV
ITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDV
DIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMKI
KIIAPPERKYSVWIGGSILASLSTFQQMWISKHEYDESGP
SIVHRKCF
S:  MGSVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTCLYGDF
FTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAA
IFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKK
GGVASGF
Description


Functional site

1) chain S
residue 43
type
sequence G
description BINDING SITE FOR RESIDUE CA S 128
source : AC1

2) chain S
residue 44
type
sequence D
description BINDING SITE FOR RESIDUE CA S 128
source : AC1

3) chain S
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE CA S 128
source : AC1

4) chain S
residue 123
type
sequence V
description BINDING SITE FOR RESIDUE CA S 128
source : AC1

5) chain A
residue 167
type
sequence E
description BINDING SITE FOR RESIDUE CA S 129
source : AC2

6) chain S
residue 87
type
sequence D
description BINDING SITE FOR RESIDUE CA S 129
source : AC2

7) chain S
residue 92
type
sequence G
description BINDING SITE FOR RESIDUE CA S 129
source : AC2

8) chain S
residue 94
type
sequence A
description BINDING SITE FOR RESIDUE CA S 129
source : AC2

9) chain A
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

10) chain A
residue 14
type
sequence S
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

11) chain A
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

12) chain A
residue 16
type
sequence M
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

13) chain A
residue 18
type
sequence K
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

14) chain A
residue 156
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

15) chain A
residue 157
type
sequence D
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

16) chain A
residue 158
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

17) chain A
residue 159
type
sequence V
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

18) chain A
residue 182
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

19) chain A
residue 210
type
sequence R
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

20) chain A
residue 213
type
sequence K
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

21) chain A
residue 214
type
sequence E
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

22) chain A
residue 301
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

23) chain A
residue 302
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

24) chain A
residue 303
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

25) chain A
residue 305
type
sequence M
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

26) chain A
residue 306
type
sequence F
description BINDING SITE FOR RESIDUE ATP A 1376
source : AC4

27) chain A
residue 53-63
type prosite
sequence YVGDEAQSKRG
description ACTINS_1 Actins signature 1. YVGDEAQs.KRG
source prosite : PS00406

28) chain A
residue 356-364
type prosite
sequence WISKHEYDE
description ACTINS_2 Actins signature 2. WISKhEYDE
source prosite : PS00432

29) chain A
residue 104-116
type prosite
sequence LLTEAPLNPKANR
description ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
source prosite : PS01132

30) chain A
residue 54
type MOD_RES
sequence V
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

31) chain S
residue 44
type MOD_RES
sequence D
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

32) chain S
residue 75
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

33) chain S
residue 87
type MOD_RES
sequence D
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

34) chain S
residue 92
type MOD_RES
sequence G
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

35) chain S
residue 94
type MOD_RES
sequence A
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

36) chain S
residue 123
type MOD_RES
sequence V
description Phosphotyrosine => ECO:0000269|PubMed:7498488
source Swiss-Prot : SWS_FT_FI1

37) chain S
residue 113
type BINDING
sequence K
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

38) chain S
residue 37
type MOD_RES
sequence Y
description Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201
source Swiss-Prot : SWS_FT_FI3


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