eF-site ID 3fwc-ABCDEFGHIJKLMNOP
PDB Code 3fwc
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P

click to enlarge
Title Sac3:Sus1:Cdc31 complex
Classification cell cycle, transcription
Compound Cell division control protein 31
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (SUS1_YEAST)
Sequence A:  SELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGF
ELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDP
LDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEEL
RAMIEEFDLDGDGEINENEFIAICT
B:  SKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFI
DTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEK
WQA
C:  QLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLT
KSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQIR
EFLEEIV
D:  AQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDL
TKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQI
REFLEE
E:  PLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKA
LGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILK
RDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTD
EELRAMIEEFDLDGDGEINENEFIAICTDS
F:  SKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFI
DTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEK
WQAS
G:  AQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDL
TKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQI
REFLEEIV
H:  MDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKV
KDLTKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVL
KQIREFLEEIVD
I:  LNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKAL
GFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKR
DPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDE
ELRAMIEEFDLDGDGEINENEFIAICT
J:  EQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRE
LYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEKWQAS
K:  AQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDL
TKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQI
REFLEEIV
L:  KSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKS
EMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQIREF
LEEI
M:  LNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKAL
GFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKR
DPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDE
ELRAMIEEFDLDGDGEINENEFIAICTD
N:  SKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFI
DTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEK
WQAS
O:  AQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDL
TKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQI
REFLEEIVD
P:  MDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKV
KDLTKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVL
KQIREFLEEIVDT
Description


Functional site

1) chain A
residue 43
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 162
source : AC1

2) chain A
residue 46
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 162
source : AC1

3) chain A
residue 58
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 162
source : AC1

4) chain B
residue 776
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 162
source : AC1

5) chain B
residue 779
type
sequence L
description BINDING SITE FOR RESIDUE SO4 A 162
source : AC1

6) chain C
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 162
source : AC1

7) chain E
residue 43
type
sequence H
description BINDING SITE FOR RESIDUE SO4 G 97
source : AC2

8) chain E
residue 58
type
sequence K
description BINDING SITE FOR RESIDUE SO4 G 97
source : AC2

9) chain F
residue 776
type
sequence R
description BINDING SITE FOR RESIDUE SO4 G 97
source : AC2

10) chain F
residue 779
type
sequence L
description BINDING SITE FOR RESIDUE SO4 G 97
source : AC2

11) chain G
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE SO4 G 97
source : AC2

12) chain I
residue 43
type
sequence H
description BINDING SITE FOR RESIDUE SO4 I 162
source : AC3

13) chain I
residue 58
type
sequence K
description BINDING SITE FOR RESIDUE SO4 I 162
source : AC3

14) chain J
residue 776
type
sequence R
description BINDING SITE FOR RESIDUE SO4 I 162
source : AC3

15) chain K
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE SO4 I 162
source : AC3

16) chain M
residue 43
type
sequence H
description BINDING SITE FOR RESIDUE SO4 M 162
source : AC4

17) chain M
residue 58
type
sequence K
description BINDING SITE FOR RESIDUE SO4 M 162
source : AC4

18) chain N
residue 776
type
sequence R
description BINDING SITE FOR RESIDUE SO4 M 162
source : AC4

19) chain N
residue 779
type
sequence L
description BINDING SITE FOR RESIDUE SO4 M 162
source : AC4

20) chain O
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE SO4 M 162
source : AC4

21) chain C
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

22) chain E
residue 33
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

23) chain L
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

24) chain E
residue 37
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

25) chain O
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

26) chain E
residue 142
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

27) chain P
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

28) chain E
residue 146
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

29) chain E
residue 148
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

30) chain E
residue 153
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

31) chain I
residue 33
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

32) chain F
residue 748
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

33) chain I
residue 35
type CROSSLNK
sequence N
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

34) chain I
residue 37
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

35) chain I
residue 44
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

36) chain I
residue 142
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

37) chain I
residue 144
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

38) chain I
residue 146
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

39) chain I
residue 148
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

40) chain I
residue 153
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

41) chain M
residue 33
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

42) chain M
residue 35
type CROSSLNK
sequence N
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

43) chain D
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

44) chain M
residue 37
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

45) chain M
residue 44
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

46) chain M
residue 142
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

47) chain M
residue 144
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

48) chain M
residue 146
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

49) chain M
residue 148
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

50) chain M
residue 153
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

51) chain N
residue 748
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

52) chain G
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 144
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

54) chain H
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

55) chain A
residue 148
type CROSSLNK
sequence E
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

56) chain K
residue 68
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI1

57) chain A
residue 130
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI2

58) chain E
residue 130
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI2

59) chain I
residue 130
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI2

60) chain M
residue 130
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI2

61) chain A
residue 33-45
type prosite
sequence DMNNDGFLDYHEL
description EF_HAND_1 EF-hand calcium-binding domain. DMNNDGFLDyhEL
source prosite : PS00018

62) chain A
residue 142-154
type prosite
sequence DLDGDGEINENEF
description EF_HAND_1 EF-hand calcium-binding domain. DMNNDGFLDyhEL
source prosite : PS00018


Display surface

Download
Links