eF-site ID 1nvu-QRS
PDB Code 1nvu
Chain Q, R, S

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Title Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS
Classification SIGNALING PROTEIN
Compound Transforming protein p21/H-RAS-1
Source null (SOS1_HUMAN)
Sequence Q:  MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSY
RKQVVIDGETCLLDILDTGGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV
REIRQH
R:  MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSY
RKQVVIDGETCLLDILDTGGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV
REIRQH
S:  QMRLPSADVYRFAEPDSEENIIFEEGIPIIKAGTVIKLIE
RLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERFEIP
EPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLN
VCRHWVEHHFYDFERDAYLLQRMEEFIGTVRGKAMKKWVE
SITKIIQRKKIAHNITFQSSPPTVEWHISRPGHIETFDLL
TLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEIN
SPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIE
ILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQ
KKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNI
LKTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQNQ
PYCLRVESDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIE
PRNPKPLPRFPKKYSYPLKSPGVRPSNPR
Description


Functional site

1) chain Q
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE MG Q 1002
source : AC1

2) chain Q
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE MG Q 1002
source : AC1

3) chain R
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

4) chain R
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

5) chain R
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

6) chain R
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

7) chain R
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

8) chain R
residue 59
type
sequence G
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

9) chain R
residue 62
type
sequence E
description BINDING SITE FOR RESIDUE PO4 R 1003
source : AC2

10) chain S
residue 625
type
sequence R
description BINDING SITE FOR RESIDUE PO4 S 1047
source : AC3

11) chain S
residue 695
type
sequence H
description BINDING SITE FOR RESIDUE PO4 S 1047
source : AC3

12) chain S
residue 699
type
sequence H
description BINDING SITE FOR RESIDUE PO4 S 1047
source : AC3

13) chain S
residue 700
type
sequence H
description BINDING SITE FOR RESIDUE PO4 S 1047
source : AC3

14) chain R
residue 63
type
sequence E
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

15) chain R
residue 127
type
sequence S
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

16) chain R
residue 128
type
sequence R
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

17) chain R
residue 131
type
sequence Q
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

18) chain S
residue 814
type
sequence K
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

19) chain S
residue 815
type
sequence E
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

20) chain S
residue 826
type
sequence R
description BINDING SITE FOR RESIDUE PO4 S 1048
source : AC4

21) chain S
residue 660
type
sequence R
description BINDING SITE FOR RESIDUE PO4 S 1049
source : AC5

22) chain S
residue 709
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 S 1049
source : AC5

23) chain S
residue 716
type
sequence E
description BINDING SITE FOR RESIDUE PO4 S 1049
source : AC5

24) chain S
residue 951
type
sequence H
description BINDING SITE FOR RESIDUE PO4 S 1049
source : AC5

25) chain Q
residue 153
type
sequence E
description BINDING SITE FOR RESIDUE PO4 Q 1007
source : AC6

26) chain Q
residue 154
type
sequence D
description BINDING SITE FOR RESIDUE PO4 Q 1007
source : AC6

27) chain Q
residue 157
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 Q 1007
source : AC6

28) chain Q
residue 161
type
sequence R
description BINDING SITE FOR RESIDUE PO4 Q 1007
source : AC6

29) chain Q
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

30) chain Q
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

31) chain Q
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

32) chain Q
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

33) chain Q
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

34) chain Q
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

35) chain Q
residue 18
type
sequence A
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

36) chain Q
residue 28
type
sequence F
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

37) chain Q
residue 29
type
sequence V
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

38) chain Q
residue 30
type
sequence D
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

39) chain Q
residue 32
type
sequence Y
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

40) chain Q
residue 34
type
sequence P
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

41) chain Q
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

42) chain Q
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

43) chain Q
residue 62
type
sequence E
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

44) chain Q
residue 116
type
sequence N
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

45) chain Q
residue 117
type
sequence K
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

46) chain Q
residue 119
type
sequence D
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

47) chain Q
residue 120
type
sequence L
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

48) chain Q
residue 145
type
sequence S
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

49) chain Q
residue 146
type
sequence A
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

50) chain Q
residue 147
type
sequence K
description BINDING SITE FOR RESIDUE GTP Q 1001
source : AC7

51) chain Q
residue 13
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

52) chain Q
residue 29
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

53) chain Q
residue 59
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

54) chain Q
residue 116
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

55) chain Q
residue 145
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

56) chain R
residue 13
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

57) chain R
residue 29
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

58) chain R
residue 145
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

59) chain R
residue 59
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

60) chain R
residue 116
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16698776
source Swiss-Prot : SWS_FT_FI1

61) chain Q
residue 1
type MOD_RES
sequence M
description N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12
source Swiss-Prot : SWS_FT_FI2

62) chain R
residue 1
type MOD_RES
sequence M
description N-acetylmethionine; in GTPase HRas; alternate => ECO:0000269|Ref.12
source Swiss-Prot : SWS_FT_FI2

63) chain Q
residue 2
type MOD_RES
sequence T
description N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12
source Swiss-Prot : SWS_FT_FI3

64) chain R
residue 2
type MOD_RES
sequence T
description N-acetylthreonine; in GTPase HRas, N-terminally processed => ECO:0000269|Ref.12
source Swiss-Prot : SWS_FT_FI3

65) chain Q
residue 118
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:9020151
source Swiss-Prot : SWS_FT_FI4

66) chain R
residue 118
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000269|PubMed:9020151
source Swiss-Prot : SWS_FT_FI4

67) chain Q
residue 35
type CARBOHYD
sequence T
description (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667
source Swiss-Prot : SWS_FT_FI5

68) chain R
residue 35
type CARBOHYD
sequence T
description (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667
source Swiss-Prot : SWS_FT_FI5

69) chain S
residue 927-960
type prosite
sequence VPFFGIYLTNILKTEEGNPEVLKRHGKELINFSK
description RASGEF Ras Guanine-nucleotide exchange factors domain signature. VPFfGiyLtNIlkteegnpevlkrhgkel.................INFsK
source prosite : PS00720


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