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a tool for identifying drug-targetable redox-active disulphides

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ZZ-type zinc finger-containing protein 3

Intramolecular
Cysteine 823 and cysteine 853
Cysteine 823 and cysteine 850
Cysteine 826 and cysteine 853
Cysteine 823 and cysteine 826
Cysteine 826 and cysteine 850
Cysteine 838 and cysteine 841
Cysteine 850 and cysteine 853
Cysteine 853 and cysteine 856
Cysteine 823 and cysteine 856
Cysteine 823 and cysteine 838
More...
Cysteine 838 and cysteine 856
Cysteine 826 and cysteine 856
Cysteine 838 and cysteine 853
Cysteine 850 and cysteine 856
A redox-regulated disulphide may form within ZZ-type zinc finger-containing protein 3 between cysteines 823 and 853.

Details

Redox score ?
86
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
14
Peptide accession
Q8IYH5
Residue number A
823
Residue number B
853
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 823 of ZZ-type zinc finger-containing protein 3

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 853 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 823 and 850.

Details

Redox score ?
84
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
24
Peptide accession
Q8IYH5
Residue number A
823
Residue number B
850
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 823 of ZZ-type zinc finger-containing protein 3

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 850 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 826 and 853.

Details

Redox score ?
83
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
Q8IYH5
Residue number A
826
Residue number B
853
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 826 of ZZ-type zinc finger-containing protein 3

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 853 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 823 and 826.

Details

Redox score ?
82
PDB code
6e86
Structure name
solution structure of zzz3 zz domain in complex with histone h3k4ac peptide
Structure deposition date
2018-07-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
15
Peptide accession
Q8IYH5
Residue number A
823
Residue number B
826
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 823 of ZZ-type zinc finger-containing protein 3

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 826 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 826 and 850.

Details

Redox score ?
81
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
10
Peptide accession
Q8IYH5
Residue number A
826
Residue number B
850
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 826 of ZZ-type zinc finger-containing protein 3

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 850 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 838 and 841.

Details

Redox score ?
81
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
36
Peptide accession
Q8IYH5
Residue number A
838
Residue number B
841
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 838 of ZZ-type zinc finger-containing protein 3

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 841 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 850 and 853.

Details

Redox score ?
74
PDB code
6e86
Structure name
solution structure of zzz3 zz domain in complex with histone h3k4ac peptide
Structure deposition date
2018-07-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
17
Peptide accession
Q8IYH5
Residue number A
850
Residue number B
853
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 850 of ZZ-type zinc finger-containing protein 3

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 853 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 853 and 856.

Details

Redox score ?
62
PDB code
6e86
Structure name
solution structure of zzz3 zz domain in complex with histone h3k4ac peptide
Structure deposition date
2018-07-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
6
Peptide accession
Q8IYH5
Residue number A
853
Residue number B
856
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 853 of ZZ-type zinc finger-containing protein 3

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 856 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 823 and 856. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
16
Peptide accession
Q8IYH5
Residue number A
823
Residue number B
856
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 823 of ZZ-type zinc finger-containing protein 3

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 856 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 823 and 838. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
6
% buried
37
Peptide accession
Q8IYH5
Residue number A
823
Residue number B
838
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 823 of ZZ-type zinc finger-containing protein 3

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 838 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 838 and 856. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
26
Peptide accession
Q8IYH5
Residue number A
838
Residue number B
856
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 838 of ZZ-type zinc finger-containing protein 3

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 856 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 826 and 856. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6e83
Structure name
solution structure of zzz3 zz domain in complex with histone h3 tail
Structure deposition date
2018-07-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
2
Peptide accession
Q8IYH5
Residue number A
826
Residue number B
856
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 826 of ZZ-type zinc finger-containing protein 3

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 856 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 838 and 853. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6e86
Structure name
solution structure of zzz3 zz domain in complex with histone h3k4ac peptide
Structure deposition date
2018-07-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
24
Peptide accession
Q8IYH5
Residue number A
838
Residue number B
853
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 838 of ZZ-type zinc finger-containing protein 3

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 853 of ZZ-type zinc finger-containing protein 3

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 ZZ-type zinc finger-containing protein 3 between cysteines 850 and 856. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6e86
Structure name
solution structure of zzz3 zz domain in complex with histone h3k4ac peptide
Structure deposition date
2018-07-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
12
Peptide accession
Q8IYH5
Residue number A
850
Residue number B
856
Peptide name
ZZ-type zinc finger-containing protein 3

Ligandability

Cysteine 850 of ZZ-type zinc finger-containing protein 3

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 856 of ZZ-type zinc finger-containing protein 3

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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