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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