eF-site ID 3vuy-ABCDEF
PDB Code 3vuy
Chain A, B, C, D, E, F

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Title Crystal structure of A20 ZF7 in complex with linear tetraubiquitin
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
D:  PPKQRCRAPACDHFGNAKCNGYCNECFQFKQMY
E:  KQRCRAPACDHFGNAKCNGYCNECFQFKQMYG
F:  KQRCRAPACDHFGNAKCNGYCNECFQFKQMY
Description


Functional site
1) chain D
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 801
source : AC1
2) chain D
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 801
source : AC1
3) chain D
residue 779
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 801
source : AC1
4) chain D
residue 782
type
sequence C
description BINDING SITE FOR RESIDUE ZN D 801
source : AC1
5) chain D
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE K D 802
source : AC2
6) chain D
residue 764
type
sequence A
description BINDING SITE FOR RESIDUE K D 802
source : AC2
7) chain D
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE K D 802
source : AC2
8) chain F
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC3
9) chain F
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC3
10) chain F
residue 779
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC3
11) chain F
residue 782
type
sequence C
description BINDING SITE FOR RESIDUE ZN F 801
source : AC3
12) chain F
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE K F 802
source : AC4
13) chain F
residue 764
type
sequence A
description BINDING SITE FOR RESIDUE K F 802
source : AC4
14) chain F
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE K F 802
source : AC4
15) chain E
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC5
16) chain E
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC5
17) chain E
residue 779
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC5
18) chain E
residue 782
type
sequence C
description BINDING SITE FOR RESIDUE ZN E 801
source : AC5
19) chain E
residue 762
type
sequence C
description BINDING SITE FOR RESIDUE K E 802
source : AC6
20) chain E
residue 764
type
sequence A
description BINDING SITE FOR RESIDUE K E 802
source : AC6
21) chain E
residue 767
type
sequence C
description BINDING SITE FOR RESIDUE K E 802
source : AC6
22) chain A
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299
23) chain D
residue 762
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
24) chain E
residue 767
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
25) chain E
residue 779
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
26) chain E
residue 782
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
27) chain D
residue 767
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
28) chain D
residue 779
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
29) chain D
residue 782
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
30) chain F
residue 762
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
31) chain F
residue 767
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
32) chain F
residue 779
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
33) chain F
residue 782
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
34) chain E
residue 762
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00451
source Swiss-Prot : SWS_FT_FI1
35) 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
36) 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
37) 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
38) 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
39) 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
40) 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
41) 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
42) 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
43) 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
44) chain A
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
45) chain C
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
46) chain B
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
47) 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
48) 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
49) 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
50) chain A
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
51) chain C
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
52) chain B
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
53) chain A
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
54) chain C
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
55) chain B
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
56) 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
57) 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
58) 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
59) 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
60) 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
61) 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
62) 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
63) 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
64) 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
65) 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
66) 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
67) 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
68) 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
69) 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
70) 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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