eF-site ID 4k7s-ABC
PDB Code 4k7s
Chain A, B, C

click to enlarge
Title Crystal structure of Zn2-hUb (human ubiquitin) adduct from a solution 35 mM zinc acetate/1.3 mM hUb
Classification LIGASE
Compound ubiquitin
Source Homo sapiens (Human) (UBC_HUMAN)
Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLV
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR
C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLR
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 B
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 101
source : AC1
4) chain A
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 102
source : AC2
5) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 102
source : AC2
6) chain A
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 103
source : AC3
7) chain A
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 103
source : AC3
8) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 103
source : AC3
9) chain B
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 103
source : AC3
10) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 103
source : AC3
11) chain A
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 101
source : AC4
12) chain B
residue 6
type
sequence K
description BINDING SITE FOR RESIDUE ZN B 101
source : AC4
13) chain B
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 101
source : AC4
14) chain B
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE ZN B 102
source : AC5
15) chain B
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 102
source : AC5
16) chain C
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 102
source : AC5
17) chain B
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE ACT B 103
source : AC6
18) chain B
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE ACT B 103
source : AC6
19) chain B
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE ACT B 103
source : AC6
20) chain B
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE ACT B 103
source : AC6
21) chain A
residue 51
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 101
source : AC7
22) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE ZN C 101
source : AC7
23) chain C
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 101
source : AC7
24) chain B
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 102
source : AC8
25) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 102
source : AC8
26) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ACT C 103
source : AC9
27) chain B
residue 21
type
sequence D
description BINDING SITE FOR RESIDUE ACT C 103
source : AC9
28) chain B
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE ACT C 103
source : AC9
29) chain C
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE ACT C 103
source : AC9
30) chain C
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO C 104
source : BC1
31) chain C
residue 8
type
sequence L
description BINDING SITE FOR RESIDUE EDO C 104
source : BC1
32) chain C
residue 69
type
sequence L
description BINDING SITE FOR RESIDUE EDO C 104
source : BC1
33) chain A
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
34) chain B
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
35) chain B
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
36) chain C
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
37) chain C
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
38) chain A
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
39) chain B
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
40) chain C
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
41) 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
42) 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
43) 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
44) chain A
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
45) chain B
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
46) chain C
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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
54) 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
55) 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
56) 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
57) 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
58) 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
59) chain A
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299
60) 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
61) 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
62) 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
63) 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
64) 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
65) 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
66) 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
67) 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
68) 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

Display surface

Download
Links