eF-site ID 4k7w-ABC
PDB Code 4k7w
Chain A, B, C

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Title Crystal structure of Zn3-hUb(human ubiquitin) adduct from a solution 100 mM zinc acetate/1.3 mM hUb
Classification LIGASE
Compound ubiquitin
Source Homo sapiens (Human) (UBC_HUMAN)
Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR
C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR
Description


Functional site

1) chain A
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE ZN A 101
source : AC1

2) chain A
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 101
source : AC1

3) chain B
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 101
source : AC1

4) chain A
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 102
source : AC2

5) chain C
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 102
source : AC2

6) chain A
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 103
source : AC3

7) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 103
source : AC3

8) chain A
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 104
source : AC4

9) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 104
source : AC4

10) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 104
source : AC4

11) chain A
residue 6
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 105
source : AC5

12) chain A
residue 66
type
sequence T
description BINDING SITE FOR RESIDUE ACT A 105
source : AC5

13) chain A
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 105
source : AC5

14) chain B
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 105
source : AC5

15) chain A
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 106
source : AC6

16) chain A
residue 17
type
sequence V
description BINDING SITE FOR RESIDUE EDO A 106
source : AC6

17) chain A
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 106
source : AC6

18) chain A
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 106
source : AC6

19) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 106
source : AC6

20) chain A
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 101
source : AC7

21) chain B
residue 6
type
sequence K
description BINDING SITE FOR RESIDUE ZN B 101
source : AC7

22) chain B
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 101
source : AC7

23) chain B
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE ZN B 102
source : AC8

24) chain B
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 102
source : AC8

25) chain C
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 102
source : AC8

26) chain A
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 101
source : AC9

27) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE ZN C 101
source : AC9

28) chain C
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 101
source : AC9

29) chain B
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 102
source : BC1

30) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 102
source : BC1

31) chain A
residue 39
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 103
source : BC2

32) chain C
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 103
source : BC2

33) chain A
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ACT C 104
source : BC3

34) chain C
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ACT C 104
source : BC3

35) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ACT C 104
source : BC3

36) chain C
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ACT C 104
source : BC3

37) chain C
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE ACT C 104
source : BC3

38) chain A
residue 39
type
sequence D
description BINDING SITE FOR RESIDUE ACT C 105
source : BC4

39) chain C
residue 6
type
sequence K
description BINDING SITE FOR RESIDUE ACT C 105
source : BC4

40) chain C
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ACT C 105
source : BC4

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

42) chain A
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

45) chain B
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

46) chain C
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

47) chain C
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

48) 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

49) 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

50) 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

51) 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

52) 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

53) 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

54) 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

55) 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

56) 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

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

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

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

60) 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

61) 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

62) 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

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

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

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

66) 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

67) 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

68) 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

69) 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

70) 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

71) 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

72) 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

73) 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

74) 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

75) 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

76) 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

77) 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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