eF-site ID 3vux-ABCEFG
PDB Code 3vux
Chain A, B, C, E, F, G

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Title Crystal structure of A20 ZF7 in complex with linear ubiquitin, form II
Classification PROTEIN BINDING/METAL BINDING PROTEIN
Compound Polyubiquitin-C
Source Homo sapiens (Human) (TNAP3_HUMAN)
Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
E:  PKQRCRAPACDHFGNAKCNGYCNECFQFKQMYG
F:  KQRCRAPACDHFGNAKCNGYCNECFQFKQMYG
G:  PPKQRCRAPACDHFGNAKCNGYCNECFQFKQMYG
Description


Functional site

1) chain A
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 101
source : AC1

2) chain A
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 101
source : AC1

3) chain A
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 101
source : AC1

4) chain G
residue 789
type
sequence Y
description BINDING SITE FOR RESIDUE EDO A 101
source : AC1

5) chain E
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC2

6) chain E
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC2

7) chain E
residue 779
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC2

8) chain E
residue 782
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC2

9) chain E
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE K E 802
source : AC3

10) chain E
residue 764
type
sequence A
description BINDING SITE FOR RESIDUE K E 802
source : AC3

11) chain E
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE K E 802
source : AC3

12) chain F
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC4

13) chain F
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC4

14) chain F
residue 779
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC4

15) chain F
residue 782
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC4

16) chain F
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE K F 802
source : AC5

17) chain F
residue 764
type
sequence A
description BINDING SITE FOR RESIDUE K F 802
source : AC5

18) chain F
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE K F 802
source : AC5

19) chain G
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE ZN G 801
source : AC6

20) chain G
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE ZN G 801
source : AC6

21) chain G
residue 779
type
sequence C
description BINDING SITE FOR RESIDUE ZN G 801
source : AC6

22) chain G
residue 782
type
sequence C
description BINDING SITE FOR RESIDUE ZN G 801
source : AC6

23) chain G
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE K G 802
source : AC7

24) chain G
residue 764
type
sequence A
description BINDING SITE FOR RESIDUE K G 802
source : AC7

25) chain G
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE K G 802
source : AC7

26) chain A
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299

27) chain E
residue 762
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

28) chain G
residue 767
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

29) chain G
residue 779
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

30) chain G
residue 782
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

31) chain E
residue 767
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

32) chain E
residue 779
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

33) chain E
residue 782
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

34) chain F
residue 762
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

35) chain F
residue 767
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

36) chain F
residue 779
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

37) chain F
residue 782
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

38) chain G
residue 762
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10

40) chain B
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10

41) chain C
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10

42) chain A
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11

43) chain B
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11

44) chain C
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11

45) chain A
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12

46) chain B
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12

47) chain C
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12

48) chain A
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

50) chain C
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3

52) chain B
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3

53) chain C
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3

54) chain A
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

55) chain B
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

56) chain C
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

57) chain A
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

58) chain B
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

59) chain C
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

60) chain A
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6

61) chain B
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6

62) chain C
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6

63) chain A
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

64) chain B
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

65) chain C
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

66) chain A
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

67) chain A
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

68) chain B
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

69) chain B
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

70) chain C
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

71) chain C
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

72) chain A
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9

73) chain B
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9

74) chain C
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9


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