E3 ubiquitin-protein ligase TRIM21
Intramolecular
Cysteine 16 and cysteine 19
Cysteine 19 and cysteine 36
Cysteine 19 and cysteine 39
Cysteine 31 and cysteine 51
Cysteine 92 and cysteine 114
Cysteine 51 and cysteine 54
Cysteine 31 and cysteine 54
Cysteine 111 and cysteine 114
Cysteine 16 and cysteine 36
Cysteine 36 and cysteine 39
More...Cysteine 92 and cysteine 111
Cysteine 92 and cysteine 103
Cysteine 103 and cysteine 114
Cysteine 103 and cysteine 111
Cysteine 16 and cysteine 39
6s53 B 16 B 19
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 16 and 19.
Details
Redox score ?
78
PDB code
6s53
Structure name
crystal structure of trim21 ring domain in complex with an isopeptide- linked ube2n~ubiquitin conjugate
Structure deposition date
2019-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
6
% buried
nan
Peptide accession
P19474
Residue number A
16
Residue number B
19
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase TRIM21
Cysteine 19 of E3 ubiquitin-protein ligase TRIM21
6s53 H 19 H 36
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 19 and 36.
Details
Redox score ?
78
PDB code
6s53
Structure name
crystal structure of trim21 ring domain in complex with an isopeptide- linked ube2n~ubiquitin conjugate
Structure deposition date
2019-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
64
Peptide accession
P19474
Residue number A
19
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 19 of E3 ubiquitin-protein ligase TRIM21
Cysteine 36 of E3 ubiquitin-protein ligase TRIM21
6fga E 19 E 39
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 19 and 39.
Details
Redox score ?
77
PDB code
6fga
Structure name
crystal structure of trim21 e3 ligase, ring domain in complex with its cognate e2 conjugating enzyme ube2e1
Structure deposition date
2018-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
70
Peptide accession
P19474
Residue number A
19
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 19 of E3 ubiquitin-protein ligase TRIM21
Cysteine 39 of E3 ubiquitin-protein ligase TRIM21
7bbd B 107 B 127
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 31 and 51 (107 and 127 respectively in this structure).
Details
Redox score ?
77
PDB code
7bbd
Structure name
crystal structure of monoubiquitinated trim21 ring (ub-ring) in complex with ubiquitin charged ube2n (ube2n~ub) and ube2v2
Structure deposition date
2020-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
72
Peptide accession
P19474
Residue number A
31
Residue number B
51
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase TRIM21
Cysteine 51 of E3 ubiquitin-protein ligase TRIM21
5olm A 92 A 114
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 92 and 114.
Details
Redox score ?
76
PDB code
5olm
Structure name
trim21
Structure deposition date
2017-07-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
nan
Peptide accession
P19474
Residue number A
92
Residue number B
114
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 92 of E3 ubiquitin-protein ligase TRIM21
Cysteine 114 of E3 ubiquitin-protein ligase TRIM21
6fga E 51 E 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 51 and 54.
Details
Redox score ?
75
PDB code
6fga
Structure name
crystal structure of trim21 e3 ligase, ring domain in complex with its cognate e2 conjugating enzyme ube2e1
Structure deposition date
2018-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
nan
Peptide accession
P19474
Residue number A
51
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 51 of E3 ubiquitin-protein ligase TRIM21
Cysteine 54 of E3 ubiquitin-protein ligase TRIM21
6fga A 31 A 54
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 31 and 54.
Details
Redox score ?
74
PDB code
6fga
Structure name
crystal structure of trim21 e3 ligase, ring domain in complex with its cognate e2 conjugating enzyme ube2e1
Structure deposition date
2018-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
43
Peptide accession
P19474
Residue number A
31
Residue number B
54
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 31 of E3 ubiquitin-protein ligase TRIM21
Cysteine 54 of E3 ubiquitin-protein ligase TRIM21
5olm B 111 B 114
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 111 and 114.
Details
Redox score ?
69
PDB code
5olm
Structure name
trim21
Structure deposition date
2017-07-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
71
Peptide accession
P19474
Residue number A
111
Residue number B
114
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 111 of E3 ubiquitin-protein ligase TRIM21
Cysteine 114 of E3 ubiquitin-protein ligase TRIM21
6s53 A 16 A 36
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 16 and 36.
Details
Redox score ?
63
PDB code
6s53
Structure name
crystal structure of trim21 ring domain in complex with an isopeptide- linked ube2n~ubiquitin conjugate
Structure deposition date
2019-06-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
14
% buried
nan
Peptide accession
P19474
Residue number A
16
Residue number B
36
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase TRIM21
Cysteine 36 of E3 ubiquitin-protein ligase TRIM21
6s53 B 36 B 39
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 36 and 39.
Details
Redox score ?
61
PDB code
6s53
Structure name
crystal structure of trim21 ring domain in complex with an isopeptide- linked ube2n~ubiquitin conjugate
Structure deposition date
2019-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
14
% buried
58
Peptide accession
P19474
Residue number A
36
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 36 of E3 ubiquitin-protein ligase TRIM21
Cysteine 39 of E3 ubiquitin-protein ligase TRIM21
5olm A 92 A 111
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 92 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5olm
Structure name
trim21
Structure deposition date
2017-07-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
18
% buried
nan
Peptide accession
P19474
Residue number A
92
Residue number B
111
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 92 of E3 ubiquitin-protein ligase TRIM21
Cysteine 111 of E3 ubiquitin-protein ligase TRIM21
5jpx A 92 A 103
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 92 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5jpx
Structure name
solution structure of the trim21 b-box2 (b2)
Structure deposition date
2016-05-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
0
Peptide accession
P19474
Residue number A
92
Residue number B
103
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 92 of E3 ubiquitin-protein ligase TRIM21
Cysteine 103 of E3 ubiquitin-protein ligase TRIM21
5olm B 103 B 114
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 103 and 114. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5olm
Structure name
trim21
Structure deposition date
2017-07-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
33
Peptide accession
P19474
Residue number A
103
Residue number B
114
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 103 of E3 ubiquitin-protein ligase TRIM21
Cysteine 114 of E3 ubiquitin-protein ligase TRIM21
5jpx A 103 A 111
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 103 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5jpx
Structure name
solution structure of the trim21 b-box2 (b2)
Structure deposition date
2016-05-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
0
Peptide accession
P19474
Residue number A
103
Residue number B
111
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 103 of E3 ubiquitin-protein ligase TRIM21
Cysteine 111 of E3 ubiquitin-protein ligase TRIM21
6fga H 16 H 39
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM21 between cysteines 16 and 39. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6fga
Structure name
crystal structure of trim21 e3 ligase, ring domain in complex with its cognate e2 conjugating enzyme ube2e1
Structure deposition date
2018-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
23
% buried
nan
Peptide accession
P19474
Residue number A
16
Residue number B
39
Peptide name
E3 ubiquitin-protein ligase TRIM21
Ligandability
Cysteine 16 of E3 ubiquitin-protein ligase TRIM21
Cysteine 39 of E3 ubiquitin-protein ligase TRIM21
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