eF-site ID 4c0a-ABCDEFGH
PDB Code 4c0a
Chain A, B, C, D, E, F, G, H

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Title Arf1(Delta1-17)in complex with BRAG2 Sec7-PH domain
Classification PROTEIN TRANSPORT
Compound IQ MOTIF AND SEC7 DOMAIN-CONTAINING PROTEIN 1
Source (ARF1_BOVIN)
Sequence A:  FSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPV
GVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEM
DFSTMELDEALRKFQAHIRVQGKAQKVERLIEAFSQRYCI
CNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKM
KLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNED
HVSQVQKVEKLIVGLGCVLSLPHRRLVCYCRLFEVPDPNK
PQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFS
LYGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFNAPNP
QDRKKFTDDLRESIAEVQEMEKHRIESELEKQ
B:  SPAFSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPD
TPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVV
DEMDFSTMELDEALRKFQAHIRVQGKAQKVERLIEAFSQR
YCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPE
RKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKT
NEDHVSQVQKVEKLIVGKLGCVLSLPHRRLVCYCRLFEVP
DPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFR
QSFSLYGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFN
APNPQDRKKFTDDLRESIAEVQEMEKHRIESELEKQK
C:  MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVE
YKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR
ERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAA
EITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQL
R
D:  MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVE
YKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR
ERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAA
EITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQL
RNQK
E:  FSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPV
GVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEM
DFSTMELDEALRKFQAHIRVQGKAQKVERLIEAFSQRYCI
CNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKM
KLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNED
HVSQVQKVEKLIVGKGCVLSLPHRRLVCYCRLFEVPDPNK
PQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFS
LYGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFNAPNP
QDRKKFTDDLRESIAEVQEMEKHRIESELEK
F:  FSNDVIRKRHYRIGLNLFNKKPEKGVQYLIERGFVPDTPV
GVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEM
DFSTMELDEALRKFQAHIRVQGKAQKVERLIEAFSQRYCI
CNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKM
KLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNED
HVSQVQKVEKLIVGKCVLSLPHRRLVCYCRLFEVPDPNKP
QKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSL
YGMQVLLFENQYYPNGIRLTSSVPGADIKVLINFNAPNPQ
DRKKFTDDLRESIAEVQEMEKHRIESELEKQ
G:  MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVE
YKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR
ERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAA
EITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQL
RN
H:  RILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEY
KNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRE
RVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAE
ITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQL
Description


Functional site

1) chain C
residue 25
type
sequence L
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

2) chain C
residue 27
type
sequence A
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

3) chain C
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

4) chain C
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

5) chain C
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

6) chain C
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

7) chain C
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

8) chain C
residue 126
type
sequence N
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

9) chain C
residue 127
type
sequence K
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

10) chain C
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

11) chain C
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

12) chain C
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

13) chain C
residue 161
type
sequence T
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

14) chain F
residue 498
type
sequence K
description BINDING SITE FOR RESIDUE G3D C 401
source : AC1

15) chain D
residue 27
type
sequence A
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

16) chain D
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

17) chain D
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

18) chain D
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

19) chain D
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

20) chain D
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

21) chain D
residue 126
type
sequence N
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

22) chain D
residue 127
type
sequence K
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

23) chain D
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

24) chain D
residue 130
type
sequence L
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

25) chain D
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

26) chain D
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

27) chain D
residue 161
type
sequence T
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

28) chain E
residue 498
type
sequence K
description BINDING SITE FOR RESIDUE G3D D 401
source : AC2

29) chain B
residue 498
type
sequence K
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

30) chain G
residue 25
type
sequence L
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

31) chain G
residue 27
type
sequence A
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

32) chain G
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

33) chain G
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

34) chain G
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

35) chain G
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

36) chain G
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

37) chain G
residue 126
type
sequence N
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

38) chain G
residue 127
type
sequence K
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

39) chain G
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

40) chain G
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

41) chain G
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

42) chain G
residue 161
type
sequence T
description BINDING SITE FOR RESIDUE G3D G 401
source : AC3

43) chain A
residue 498
type
sequence K
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

44) chain H
residue 25
type
sequence L
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

45) chain H
residue 27
type
sequence A
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

46) chain H
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

47) chain H
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

48) chain H
residue 30
type
sequence K
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

49) chain H
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

50) chain H
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

51) chain H
residue 126
type
sequence N
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

52) chain H
residue 127
type
sequence K
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

53) chain H
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

54) chain H
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

55) chain H
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

56) chain H
residue 161
type
sequence T
description BINDING SITE FOR RESIDUE G3D H 401
source : AC4

57) chain C
residue 24
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

58) chain H
residue 24
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

59) chain H
residue 126
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

60) chain H
residue 160
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

61) chain C
residue 126
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

62) chain C
residue 160
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

63) chain D
residue 24
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

64) chain D
residue 126
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

65) chain D
residue 160
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

66) chain G
residue 24
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

67) chain G
residue 126
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

68) chain G
residue 160
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:24058294, ECO:0007744|PDB:1R8Q, ECO:0007744|PDB:1R8S, ECO:0007744|PDB:1S9D, ECO:0007744|PDB:4C0A
source Swiss-Prot : SWS_FT_FI1

69) chain A
residue 515
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI2

70) chain B
residue 515
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI2

71) chain E
residue 515
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI2

72) chain F
residue 515
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI2


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