eF-site ID 6a5s-ABCDEFGH
PDB Code 6a5s
Chain A, B, C, D, E, F, G, H

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Title Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif
Classification TRANSCRIPTION
Compound 14-3-3 protein gamma
Source (6A5S)
Sequence A:  VDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEE
RNLLSVAYKNVVGARRSSWRVISSIEQKTNEKKIEMVRAY
REKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLK
MKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHM
QPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAI
AELDTLNEDSYKDSTLIMQLLRDNLTLWTS
B:  DREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEER
NLLSVAYKNVVGARRSSWRVISSIEQKTNEKKIEMVRAYR
EKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKM
KGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQ
PTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIA
ELDTLNEDSYKDSTLIMQLLRDNLTLWTS
C:  VTSSXCPADLT
D:  DREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEER
NLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMV
RAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVF
YLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISK
EHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFD
DAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTS
E:  VTSSXCPADLT
F:  VTSSXCPADLT
G:  DREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEER
NLLSVAYKNVVGARRSSWRVISSIEQKTEKKIEMVRAYRE
KIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMK
GDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQP
THPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAE
LDTLNEDSYKDSTLIMQLLRDNLTLWTS
H:  VTSSXCPADLT
Description


Functional site

1) chain A
residue 120
type
sequence K
description binding site for residue NA A 301
source : AC1

2) chain B
residue 202
type
sequence D
description binding site for residue MG B 301
source : AC2

3) chain B
residue 203
type
sequence D
description binding site for residue MG B 301
source : AC2

4) chain B
residue 204
type
sequence A
description binding site for residue MG B 301
source : AC2

5) chain B
residue 205
type
sequence I
description binding site for residue MG B 301
source : AC2

6) chain B
residue 206
type
sequence A
description binding site for residue MG B 301
source : AC2

7) chain B
residue 50
type
sequence K
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

8) chain B
residue 57
type
sequence R
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

9) chain B
residue 132
type
sequence R
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

10) chain B
residue 133
type
sequence Y
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

11) chain B
residue 174
type
sequence G
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

12) chain B
residue 177
type
sequence L
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

13) chain B
residue 178
type
sequence N
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

14) chain B
residue 225
type
sequence L
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

15) chain C
residue 5
type
sequence S
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

16) chain C
residue 8
type
sequence P
description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
source : AC3

17) chain A
residue 50
type
sequence K
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

18) chain A
residue 57
type
sequence R
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

19) chain A
residue 132
type
sequence R
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

20) chain A
residue 133
type
sequence Y
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

21) chain A
residue 174
type
sequence G
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

22) chain A
residue 177
type
sequence L
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

23) chain A
residue 178
type
sequence N
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

24) chain A
residue 225
type
sequence L
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

25) chain E
residue 5
type
sequence S
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

26) chain E
residue 8
type
sequence P
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

27) chain E
residue 9
type
sequence A
description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
source : AC4

28) chain D
residue 50
type
sequence K
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

29) chain D
residue 57
type
sequence R
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

30) chain D
residue 132
type
sequence R
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

31) chain D
residue 133
type
sequence Y
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

32) chain D
residue 174
type
sequence G
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

33) chain D
residue 177
type
sequence L
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

34) chain D
residue 178
type
sequence N
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

35) chain F
residue 5
type
sequence S
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

36) chain F
residue 8
type
sequence P
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

37) chain F
residue 9
type
sequence A
description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
source : AC5

38) chain G
residue 50
type
sequence K
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

39) chain G
residue 57
type
sequence R
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

40) chain G
residue 132
type
sequence R
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

41) chain G
residue 133
type
sequence Y
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

42) chain G
residue 174
type
sequence G
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

43) chain G
residue 177
type
sequence L
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

44) chain G
residue 178
type
sequence N
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

45) chain H
residue 5
type
sequence S
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

46) chain H
residue 8
type
sequence P
description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
source : AC6

47) chain A
residue 42-52
type prosite
sequence RNLLSVAYKNV
description 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
source prosite : PS00796

48) chain A
residue 216-235
type prosite
sequence YKDSTLIMQLLRDNLTLWTS
description 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
source prosite : PS00797

49) chain A
residue 57
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 132
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

51) chain B
residue 57
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

52) chain B
residue 132
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

53) chain D
residue 57
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

54) chain D
residue 132
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

55) chain G
residue 57
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

56) chain G
residue 132
type SITE
sequence R
description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
source Swiss-Prot : SWS_FT_FI1

57) chain A
residue 2
type MOD_RES
sequence V
description N-acetylvaline; partial => ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330
source Swiss-Prot : SWS_FT_FI3

58) chain D
residue 71
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

59) chain A
residue 133
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI5

60) chain B
residue 133
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI5

61) chain D
residue 133
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI5

62) chain G
residue 133
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI5

63) chain A
residue 145
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|Ref.7
source Swiss-Prot : SWS_FT_FI6

64) chain B
residue 145
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|Ref.7
source Swiss-Prot : SWS_FT_FI6

65) chain D
residue 145
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|Ref.7
source Swiss-Prot : SWS_FT_FI6

66) chain G
residue 145
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|Ref.7
source Swiss-Prot : SWS_FT_FI6

67) chain A
residue 215
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI7

68) chain B
residue 215
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI7

69) chain D
residue 215
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI7

70) chain G
residue 215
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P61983
source Swiss-Prot : SWS_FT_FI7

71) chain A
residue 234
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8

72) chain B
residue 234
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8

73) chain D
residue 234
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8

74) chain G
residue 234
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8

75) chain A
residue 235
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

76) chain B
residue 235
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

77) chain D
residue 235
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

78) chain G
residue 235
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9


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