ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein DPF3

Intramolecular
Cysteine 360 and cysteine 363
Cysteine 284 and cysteine 316
Cysteine 284 and cysteine 287
Cysteine 284 and cysteine 313
Cysteine 262 and cysteine 265
Cysteine 319 and cysteine 345
Cysteine 262 and cysteine 295
Cysteine 334 and cysteine 337
Cysteine 287 and cysteine 316
Cysteine 319 and cysteine 322
More...
Cysteine 337 and cysteine 363
Cysteine 334 and cysteine 363
Cysteine 322 and cysteine 345
Cysteine 287 and cysteine 313
Cysteine 334 and cysteine 360
Cysteine 337 and cysteine 360
Cysteine 265 and cysteine 295
Cysteine 313 and cysteine 316
Cysteine 319 and cysteine 360
A redox-regulated disulphide may form within Zinc finger protein DPF3 between cysteines 360 and 363.

Details

Redox score ?
98
PDB code
5szb
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
0
% buried
36
Peptide accession
Q92784
Residue number A
360
Residue number B
363
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 360 of Zinc finger protein DPF3

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 363 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 284 and 316.

Details

Redox score ?
88
PDB code
5szc
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with monomethylated k4 and acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
3
% buried
38
Peptide accession
Q92784
Residue number A
284
Residue number B
316
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 284 of Zinc finger protein DPF3

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 316 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 284 and 287.

Details

Redox score ?
87
PDB code
5szc
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with monomethylated k4 and acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
3
% buried
34
Peptide accession
Q92784
Residue number A
284
Residue number B
287
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 284 of Zinc finger protein DPF3

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 287 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 284 and 313.

Details

Redox score ?
87
PDB code
5szc
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with monomethylated k4 and acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
53
Peptide accession
Q92784
Residue number A
284
Residue number B
313
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 284 of Zinc finger protein DPF3

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 313 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 262 and 265.

Details

Redox score ?
85
PDB code
5szb
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
24
Peptide accession
Q92784
Residue number A
262
Residue number B
265
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 262 of Zinc finger protein DPF3

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 265 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 319 and 345.

Details

Redox score ?
79
PDB code
5szb
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
20
Peptide accession
Q92784
Residue number A
319
Residue number B
345
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 319 of Zinc finger protein DPF3

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 345 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 262 and 295.

Details

Redox score ?
78
PDB code
5szc
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with monomethylated k4 and acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
34
Peptide accession
Q92784
Residue number A
262
Residue number B
295
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 262 of Zinc finger protein DPF3

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 295 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 334 and 337.

Details

Redox score ?
76
PDB code
5szc
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with monomethylated k4 and acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
61
Peptide accession
Q92784
Residue number A
334
Residue number B
337
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 334 of Zinc finger protein DPF3

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 337 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 287 and 316.

Details

Redox score ?
76
PDB code
5szc
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with monomethylated k4 and acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
26
Peptide accession
Q92784
Residue number A
287
Residue number B
316
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 287 of Zinc finger protein DPF3

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 316 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 319 and 322.

Details

Redox score ?
76
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
319
Residue number B
322
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 319 of Zinc finger protein DPF3

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 322 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 337 and 363.

Details

Redox score ?
75
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
337
Residue number B
363
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 337 of Zinc finger protein DPF3

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 363 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 334 and 363.

Details

Redox score ?
74
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
334
Residue number B
363
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 334 of Zinc finger protein DPF3

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 363 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 322 and 345.

Details

Redox score ?
74
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
322
Residue number B
345
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 322 of Zinc finger protein DPF3

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 345 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 287 and 313.

Details

Redox score ?
73
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
287
Residue number B
313
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 287 of Zinc finger protein DPF3

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 313 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 334 and 360.

Details

Redox score ?
72
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
334
Residue number B
360
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 334 of Zinc finger protein DPF3

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 360 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 337 and 360.

Details

Redox score ?
72
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
337
Residue number B
360
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 337 of Zinc finger protein DPF3

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 360 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 265 and 295.

Details

Redox score ?
71
PDB code
5i3l
Structure name
dpf3b in complex with h3k14ac peptide
Structure deposition date
2016-02-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q92784
Residue number A
265
Residue number B
295
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 265 of Zinc finger protein DPF3

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 295 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 313 and 316.

Details

Redox score ?
71
PDB code
5szb
Structure name
structure of human dpf3 double-phd domain bound to histone h3 tail peptide with acetylated k14
Structure deposition date
2016-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
44
Peptide accession
Q92784
Residue number A
313
Residue number B
316
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 313 of Zinc finger protein DPF3

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 316 of Zinc finger protein DPF3

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 Zinc finger protein DPF3 between cysteines 319 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2kwo
Structure name
solution structure of the double phd (plant homeodomain) fingers of human transcriptional protein dpf3b bound to a histone h4 peptide containing n-terminal acetylation at serine 1
Structure deposition date
2010-04-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
nan
Peptide accession
Q92784
Residue number A
319
Residue number B
360
Peptide name
Zinc finger protein DPF3

Ligandability

Cysteine 319 of Zinc finger protein DPF3

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 360 of Zinc finger protein DPF3

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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