eF-site ID 6d5v-QRS
PDB Code 6d5v
Chain Q, R, S

click to enlarge
Title Ras:SOS:Ras in complex with a small molecule activator
Classification SIGNALING PROTEIN
Compound GTPase HRas
Source (SOS1_HUMAN)
Sequence Q:  MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSY
RKQVVIDGETCLLDILDTAGQEEASAMRDQYMRTGEGFLC
VFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLV
REIRQH
R:  GMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDS
YRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCD
LAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTL
VREIRQH
S:  QMRLPSADVYRFAEPDSEENIIFEEGIPIIKAGTVIKLIE
RLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERFEIP
EPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLN
VCRHWVEHHFYDFERDAYLLQRMEEFIGTVRGKAMKKWVE
SITKIIQRKKIANITFQSSPPTVEWHISRPGHIETFDLLT
LHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINS
PNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEI
LQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQK
KILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNIL
KTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQNQP
YCLRVESDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIEP
RNPKPLPRFPKKYSYPLKSPGVRPSNP
Description


Functional site

1) chain Q
residue 17
type
sequence S
description binding site for residue MG Q 201
source : AC1

2) chain Q
residue 35
type
sequence T
description binding site for residue MG Q 201
source : AC1

3) chain Q
residue 12
type
sequence G
description binding site for residue GNP Q 202
source : AC2

4) chain Q
residue 13
type
sequence G
description binding site for residue GNP Q 202
source : AC2

5) chain Q
residue 14
type
sequence V
description binding site for residue GNP Q 202
source : AC2

6) chain Q
residue 15
type
sequence G
description binding site for residue GNP Q 202
source : AC2

7) chain Q
residue 16
type
sequence K
description binding site for residue GNP Q 202
source : AC2

8) chain Q
residue 17
type
sequence S
description binding site for residue GNP Q 202
source : AC2

9) chain Q
residue 18
type
sequence A
description binding site for residue GNP Q 202
source : AC2

10) chain Q
residue 28
type
sequence F
description binding site for residue GNP Q 202
source : AC2

11) chain Q
residue 29
type
sequence V
description binding site for residue GNP Q 202
source : AC2

12) chain Q
residue 30
type
sequence D
description binding site for residue GNP Q 202
source : AC2

13) chain Q
residue 31
type
sequence E
description binding site for residue GNP Q 202
source : AC2

14) chain Q
residue 34
type
sequence P
description binding site for residue GNP Q 202
source : AC2

15) chain Q
residue 35
type
sequence T
description binding site for residue GNP Q 202
source : AC2

16) chain Q
residue 60
type
sequence G
description binding site for residue GNP Q 202
source : AC2

17) chain Q
residue 61
type
sequence Q
description binding site for residue GNP Q 202
source : AC2

18) chain Q
residue 116
type
sequence N
description binding site for residue GNP Q 202
source : AC2

19) chain Q
residue 117
type
sequence K
description binding site for residue GNP Q 202
source : AC2

20) chain Q
residue 119
type
sequence D
description binding site for residue GNP Q 202
source : AC2

21) chain Q
residue 120
type
sequence L
description binding site for residue GNP Q 202
source : AC2

22) chain Q
residue 145
type
sequence S
description binding site for residue GNP Q 202
source : AC2

23) chain Q
residue 146
type
sequence A
description binding site for residue GNP Q 202
source : AC2

24) chain Q
residue 147
type
sequence K
description binding site for residue GNP Q 202
source : AC2

25) chain S
residue 852
type
sequence V
description binding site for residue FVY S 1101
source : AC3

26) chain S
residue 878
type
sequence M
description binding site for residue FVY S 1101
source : AC3

27) chain S
residue 879
type
sequence N
description binding site for residue FVY S 1101
source : AC3

28) chain S
residue 883
type
sequence V
description binding site for residue FVY S 1101
source : AC3

29) chain S
residue 884
type
sequence Y
description binding site for residue FVY S 1101
source : AC3

30) chain S
residue 886
type
sequence L
description binding site for residue FVY S 1101
source : AC3

31) chain S
residue 889
type
sequence T
description binding site for residue FVY S 1101
source : AC3

32) chain S
residue 890
type
sequence F
description binding site for residue FVY S 1101
source : AC3

33) chain S
residue 893
type
sequence I
description binding site for residue FVY S 1101
source : AC3

34) chain S
residue 901
type
sequence L
description binding site for residue FVY S 1101
source : AC3

35) chain S
residue 902
type
sequence E
description binding site for residue FVY S 1101
source : AC3

36) chain S
residue 905
type
sequence H
description binding site for residue FVY S 1101
source : AC3

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

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

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

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

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

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

43) 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

44) 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

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

46) 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


Display surface

Download
Links