eF-site ID 4dhj-ABCDEFGHIJKLMN
PDB Code 4dhj
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N

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Title The structure of a ceOTUB1 ubiquitin aldehyde UBC13~Ub complex
Classification HYDROLASE/SIGNALING PROTEIN/LIGASE
Compound Ubiquitin thioesterase otubain-like
Source Caenorhabditis elegans (UBE2N_HUMAN)
Sequence A:  DQQLKTIEDEQKSVPLVATLAPFSILCAEYDNETSAAFLS
KATELSEVYGEIRYIRGDGNCFYRAILVGLIEIMLKDRAR
LEKFIASSRDWTRTLVELGFPDWTCTDFCDFFIEFLEKIH
SGVHTEEAVYTILNDDGSANYILMFFRLITSAFLKQNSEE
YAPFIDEGMTVAQYCEQEIEPMWKDADHLAINSLIKAAGT
RVRIEYMDRTAAPNGGWHYDIPSDDQQIAPEITLLYRPGH
YDVIYKKD
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX
C:  GLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGP
QDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDK
LGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLA
NDVAEQWKTNEAQAIETARAWTRLYAMNN
D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVL
E:  LKTIEDEQKSVPLVATLAPFSILCAEYDNETSAAFLSKAT
ELSEVYGEIRYIRGDGNCFYRAILVGLIEIMLKDRARLEK
FIASSRDWTRTLVELGFPDWTCTDFCDFFIEFLEKIHSGV
HTEEAVYTILNDDGSANYILMFFRLITSAFLKQNSEEYAP
FIDEGMTVAQYCEQEIEPMWKDADHLAINSLIKAAGTRVR
IEYMDRTAAPNGGWHYDIPSDDQQIAPEITLLYRPGHYDV
IYKKD
F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX
G:  GLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGP
QDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDK
LGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLA
NDVAEQWKTNEAQAIETARAWTRLYAMN
H:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVL
I:  DEQKSVPLVATLAPFSILCAEYDNETSAAFLSKATELSEV
YGEIRYIRGDGNCFYRAILVGLIEIMLKDRARLEKFIASS
RDWTRTLVELGFPDWTCTDFCDFFIEFLEKIHSGVHTEEA
VYTILNDDGSANYILMFFRLITSAFLKQNSEEYAPFIDEG
MTVAQYCEQEIEPMWKDADHLAINSLIKAAGTRVRIEYMD
RTAAPNGGWHYDIPSDDQQIAPEITLLYRPGHYDVIYKKD
S
J:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX
K:  GLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGP
QDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDK
LGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLA
NDVAEQWKTNEAQAIETARAWTRLYAMN
L:  QKSVPLVATLAPFSILCAEYDNETSAAFLSKATELSEVYG
EIRYIRGDGNCFYRAILVGLIEIMLKDRARLEKFIASSRD
WTRTLVELGFPDWTCTDFCDFFIEFLEKIHSGVHTEEAVY
TILNDDGSANYILMFFRLITSAFLKQNSEEYAPFIDEGMT
VAQYCEQEIEPMWKDADHLAINSLIKAAGTRVRIEYMDRT
AAPNGGWHYDIPSDDQQIAPEITLLYRPGHYDVIYKKDS
M:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX
N:  AGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAG
PQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVD
KLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPL
ANDVAEQWKTNEAQAIETARAWTRLYAMNN
Description (1)  Ubiquitin thioesterase otubain-like (E.C.3.4.19.12), Ubiquitin aldehyde, Ubiquitin-conjugating enzyme E2 N (E.C.6.3.2.19)


Functional site

1) chain B
residue 527-552
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299

2) chain D
residue 527-552
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299

3) chain C
residue 76-91
type prosite
sequence YHPNVDKLGRICLDIL
description UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVdkl.GrICLdiL
source prosite : PS00183

4) chain B
residue 527
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

5) chain F
residue 527
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

6) chain J
residue 527
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

7) chain M
residue 527
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

8) chain B
residue 529
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

9) chain F
residue 529
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

10) chain J
residue 529
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

11) chain M
residue 529
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

12) chain B
residue 533
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

13) chain F
residue 533
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

14) chain J
residue 533
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

15) chain M
residue 533
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

16) chain B
residue 563
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

17) chain F
residue 563
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

18) chain J
residue 563
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

19) chain M
residue 563
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

20) chain B
residue 554
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 572
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

22) chain F
residue 554
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

23) chain F
residue 572
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

24) chain J
residue 554
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

25) chain J
residue 572
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

26) chain M
residue 554
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

27) chain M
residue 572
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 568
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

29) chain F
residue 568
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

30) chain J
residue 568
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

31) chain M
residue 568
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 506
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

33) chain F
residue 506
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 J
residue 506
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 M
residue 506
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

36) chain B
residue 576
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

37) chain F
residue 576
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

38) chain J
residue 576
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

39) chain M
residue 576
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7

40) chain B
residue 511
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

41) chain B
residue 548
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

42) chain F
residue 511
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

43) chain F
residue 548
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

44) chain J
residue 511
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

45) chain J
residue 548
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

46) chain M
residue 511
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

47) chain M
residue 548
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

48) chain B
residue 576
type MOD_RES
sequence X
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

49) chain F
residue 576
type MOD_RES
sequence X
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

50) chain J
residue 576
type MOD_RES
sequence X
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

51) chain M
residue 576
type MOD_RES
sequence X
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5

52) chain B
residue 566
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

53) chain F
residue 566
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

54) chain J
residue 566
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

55) chain M
residue 566
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4

56) chain B
residue 565
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

57) chain F
residue 565
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

58) chain J
residue 565
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

59) chain M
residue 565
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

60) chain G
residue 92
type MOD_RES
sequence K
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 N
residue 92
type MOD_RES
sequence K
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


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