eF-site ID 4bos-ABCEF
PDB Code 4bos
Chain A, B, C, E, F

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Title Structure of OTUD2 OTU domain in complex with Ubiquitin K11-linked peptide
Classification HYDROLASE
Compound UBIQUITIN THIOESTERASE OTU1
Source (4BOS)
Sequence A:  GPVLTRTVVPADNSALFTSVYYVVEGGVLNPACAPEMRRL
IAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEI
SILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDG
IHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEAR
RRRQ
B:  GPVLTRTVVPADNSALFTSVYYVVEGGVLNPACAPEMRRL
IAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEI
SILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDG
IHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEAR
RRRQ
C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
F:  TLTGKTI
Description


Functional site

1) chain A
residue 212
type
sequence W
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

2) chain B
residue 156
type
sequence A
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

3) chain B
residue 157
type
sequence D
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

4) chain B
residue 158
type
sequence N
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

5) chain B
residue 159
type
sequence S
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

6) chain B
residue 160
type
sequence A
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

7) chain B
residue 267
type
sequence H
description BINDING SITE FOR RESIDUE NO3 B 1310
source : AC1

8) chain B
residue 263
type
sequence Y
description BINDING SITE FOR RESIDUE NO3 B 1311
source : AC2

9) chain B
residue 265
type
sequence G
description BINDING SITE FOR RESIDUE NO3 B 1311
source : AC2

10) chain B
residue 251
type
sequence E
description BINDING SITE FOR RESIDUE MG B 1312
source : AC3

11) chain B
residue 251
type
sequence E
description BINDING SITE FOR RESIDUE MG B 1312
source : AC3

12) chain B
residue 251
type
sequence E
description BINDING SITE FOR RESIDUE MG B 1312
source : AC3

13) chain C
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE NO3 C 1077
source : AC4

14) chain A
residue 222
type
sequence A
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

15) chain C
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

16) chain C
residue 8
type
sequence L
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

17) chain C
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

18) chain C
residue 69
type
sequence L
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

19) chain C
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

20) chain C
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE NO3 C 1078
source : AC5

21) chain A
residue 267
type
sequence H
description BINDING SITE FOR RESIDUE NO3 F 1014
source : AC6

22) chain A
residue 306
type
sequence R
description BINDING SITE FOR RESIDUE NO3 F 1014
source : AC6

23) chain A
residue 307
type
sequence R
description BINDING SITE FOR RESIDUE NO3 F 1014
source : AC6

24) chain F
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE NO3 F 1014
source : AC6

25) chain F
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE NO3 F 1014
source : AC6

26) chain F
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE NO3 F 1014
source : AC6

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

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

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

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

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

32) 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

33) chain E
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

34) 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

35) chain E
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

36) 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

37) chain E
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

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

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

40) 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

41) chain E
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

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

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

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

45) 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

46) chain E
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

47) 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

48) 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

49) 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

50) chain E
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

51) chain E
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

52) 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

53) chain E
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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