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E3 ubiquitin-protein ligase MYCBP2

Intramolecular
Cysteine 4587 and cysteine 4672
Cysteine 4638 and cysteine 4652
Cysteine 4544 and cysteine 4575
Cysteine 4475 and cysteine 4478
Cysteine 4446 and cysteine 4478
Cysteine 4587 and cysteine 4669
Cysteine 1745 and cysteine 1860
Cysteine 4544 and cysteine 4547
Cysteine 4617 and cysteine 4620
Cysteine 4446 and cysteine 4475
More...
Cysteine 4544 and cysteine 4578
Cysteine 4603 and cysteine 4652
Cysteine 4599 and cysteine 4617
Cysteine 4547 and cysteine 4578
Cysteine 4575 and cysteine 4578
Cysteine 4602 and cysteine 4617
Cysteine 4669 and cysteine 4672
Cysteine 4428 and cysteine 4431
Cysteine 4431 and cysteine 4454
Cysteine 4547 and cysteine 4575
Cysteine 4603 and cysteine 4638
Cysteine 4599 and cysteine 4620
Cysteine 4602 and cysteine 4620
Cysteine 4455 and cysteine 4475
Cysteine 4428 and cysteine 4454
Cysteine 4602 and cysteine 4603
Cysteine 4428 and cysteine 4455
Cysteine 4454 and cysteine 4455
Cysteine 4446 and cysteine 4455
Cysteine 4602 and cysteine 4652
Cysteine 4599 and cysteine 4603
Cysteine 4599 and cysteine 4602
Cysteine 4431 and cysteine 4455
Cysteine 4603 and cysteine 4620
Cysteine 4599 and cysteine 4610
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4587 and 4672 (4549 and 4634 respectively in this structure).

Details

Redox score ?
88
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
0
Peptide accession
O75592
Residue number A
4587
Residue number B
4672
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4587 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4672 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4638 and 4652 (4600 and 4614 respectively in this structure).

Details

Redox score ?
85
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
19
Peptide accession
O75592
Residue number A
4638
Residue number B
4652
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4638 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4652 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4544 and 4575 (4506 and 4537 respectively in this structure).

Details

Redox score ?
84
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
3
% buried
60
Peptide accession
O75592
Residue number A
4544
Residue number B
4575
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4544 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4575 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4475 and 4478 (4437 and 4440 respectively in this structure).

Details

Redox score ?
83
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
14
Peptide accession
O75592
Residue number A
4475
Residue number B
4478
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4475 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4478 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4446 and 4478 (4408 and 4440 respectively in this structure).

Details

Redox score ?
82
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
8
Peptide accession
O75592
Residue number A
4446
Residue number B
4478
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4446 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4478 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4587 and 4669 (4549 and 4631 respectively in this structure).

Details

Redox score ?
82
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
12
Peptide accession
O75592
Residue number A
4587
Residue number B
4669
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4587 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4669 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 1745 and 1860.

Details

Redox score ?
81
PDB code
3hwj
Structure name
crystal structure of the second phr domain of mouse myc-binding protein 2 (mycbp-2)
Structure deposition date
2009-06-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q7TPH6
Residue number A
1745
Residue number B
1860
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 1745 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1860 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4544 and 4547 (4506 and 4509 respectively in this structure).

Details

Redox score ?
81
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
33
Peptide accession
O75592
Residue number A
4544
Residue number B
4547
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4544 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4547 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4617 and 4620 (4579 and 4582 respectively in this structure).

Details

Redox score ?
79
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
6
% buried
84
Peptide accession
O75592
Residue number A
4617
Residue number B
4620
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4617 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4620 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4446 and 4475 (4408 and 4437 respectively in this structure).

Details

Redox score ?
78
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
38
Peptide accession
O75592
Residue number A
4446
Residue number B
4475
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4446 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4475 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4544 and 4578 (4506 and 4540 respectively in this structure).

Details

Redox score ?
77
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
30
Peptide accession
O75592
Residue number A
4544
Residue number B
4578
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4544 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4578 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4603 and 4652 (4565 and 4614 respectively in this structure).

Details

Redox score ?
77
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
40
Peptide accession
O75592
Residue number A
4603
Residue number B
4652
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4603 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4652 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4599 and 4617 (4561 and 4579 respectively in this structure).

Details

Redox score ?
76
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
6
% buried
nan
Peptide accession
O75592
Residue number A
4599
Residue number B
4617
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4599 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4617 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4547 and 4578 (4509 and 4540 respectively in this structure).

Details

Redox score ?
76
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
22
Peptide accession
O75592
Residue number A
4547
Residue number B
4578
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4547 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4578 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4575 and 4578 (4537 and 4540 respectively in this structure).

Details

Redox score ?
75
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
42
Peptide accession
O75592
Residue number A
4575
Residue number B
4578
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4575 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4578 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4602 and 4617 (4564 and 4579 respectively in this structure).

Details

Redox score ?
75
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
6
% buried
94
Peptide accession
O75592
Residue number A
4602
Residue number B
4617
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4602 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4617 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4669 and 4672 (4631 and 4634 respectively in this structure).

Details

Redox score ?
74
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
17
Peptide accession
O75592
Residue number A
4669
Residue number B
4672
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4669 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4672 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4428 and 4431 (4390 and 4393 respectively in this structure).

Details

Redox score ?
74
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
nan
Peptide accession
O75592
Residue number A
4428
Residue number B
4431
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4428 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4431 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4431 and 4454 (4393 and 4416 respectively in this structure).

Details

Redox score ?
74
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
58
Peptide accession
O75592
Residue number A
4431
Residue number B
4454
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4431 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4454 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4547 and 4575 (4509 and 4537 respectively in this structure).

Details

Redox score ?
74
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
44
Peptide accession
O75592
Residue number A
4547
Residue number B
4575
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4547 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4575 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4603 and 4638 (4565 and 4600 respectively in this structure).

Details

Redox score ?
72
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
29
Peptide accession
O75592
Residue number A
4603
Residue number B
4638
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4603 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4638 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4599 and 4620 (4561 and 4582 respectively in this structure).

Details

Redox score ?
62
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
14
% buried
nan
Peptide accession
O75592
Residue number A
4599
Residue number B
4620
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4599 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4620 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4602 and 4620 (4564 and 4582 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
15
% buried
84
Peptide accession
O75592
Residue number A
4602
Residue number B
4620
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4602 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4620 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4455 and 4475 (4417 and 4437 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
44
Peptide accession
O75592
Residue number A
4455
Residue number B
4475
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4455 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4475 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4428 and 4454 (4390 and 4416 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
18
% buried
nan
Peptide accession
O75592
Residue number A
4428
Residue number B
4454
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4428 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4454 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4602 and 4603 (4564 and 4565 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
66
Peptide accession
O75592
Residue number A
4602
Residue number B
4603
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4602 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4603 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4428 and 4455 (4390 and 4417 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
nan
Peptide accession
O75592
Residue number A
4428
Residue number B
4455
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4428 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4455 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4454 and 4455 (4416 and 4417 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
68
Peptide accession
O75592
Residue number A
4454
Residue number B
4455
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4454 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4455 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4446 and 4455 (4408 and 4417 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
48
Peptide accession
O75592
Residue number A
4446
Residue number B
4455
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4446 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4455 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4602 and 4652 (4564 and 4614 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
7
% buried
60
Peptide accession
O75592
Residue number A
4602
Residue number B
4652
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4602 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4652 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4599 and 4603 (4561 and 4565 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
9
% buried
nan
Peptide accession
O75592
Residue number A
4599
Residue number B
4603
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4599 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4603 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4599 and 4602 (4561 and 4564 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
23
% buried
nan
Peptide accession
O75592
Residue number A
4599
Residue number B
4602
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4599 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4602 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4431 and 4455 (4393 and 4417 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
63
Peptide accession
O75592
Residue number A
4431
Residue number B
4455
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4431 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4455 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4603 and 4620 (4565 and 4582 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5o6c
Structure name
crystal structure of a threonine-selective rcr e3 ligase
Structure deposition date
2017-06-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
56
Peptide accession
O75592
Residue number A
4603
Residue number B
4620
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4603 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4620 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase MYCBP2 between cysteines 4599 and 4610 (4561 and 4572 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6t7f
Structure name
rcr e3 ligase e2-ubiquitin transthiolation intermediate
Structure deposition date
2019-10-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
nan
Peptide accession
O75592
Residue number A
4599
Residue number B
4610
Peptide name
E3 ubiquitin-protein ligase MYCBP2

Ligandability

Cysteine 4599 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 4610 of E3 ubiquitin-protein ligase MYCBP2

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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