eF-site ID 3h7s-AB
PDB Code 3h7s
Chain A, B

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Title Crystal structures of K63-linked di- and tri-ubiquitin reveal a highly extended chain architecture
Classification SIGNALING PROTEIN
Compound Ubiquitin
Source (UBIQ_HUMAN)
Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG
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 A
residue 32
type
sequence D
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 A
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 102
source : AC2

6) chain A
residue 24
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 103
source : AC3

7) chain A
residue 52
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 103
source : AC3

8) chain A
residue 6
type
sequence K
description BINDING SITE FOR RESIDUE ZN A 104
source : AC4

9) chain A
residue 64
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 104
source : AC4

10) chain A
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 104
source : AC4

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

12) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 101
source : AC7

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

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

15) chain B
residue 52
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 102
source : AC8

16) chain B
residue 64
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 103
source : AC9

17) chain B
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 103
source : AC9

18) chain B
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE ZN B 104
source : BC1

19) chain B
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 104
source : BC1

20) chain B
residue 32
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 104
source : BC1

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

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

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

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

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

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

27) 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

28) 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

29) 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

30) 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

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

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

33) 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

34) 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

35) 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

36) 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

37) 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

38) 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

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

40) 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

41) 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

42) 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

43) 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

44) 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

45) 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


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