ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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PHD finger protein 6

Intermolecular
Cysteine 283 and cysteine 283 L
Intramolecular
Cysteine 292 and cysteine 297 L
Cysteine 297 and cysteine 326
Cysteine 292 and cysteine 326 L
Cysteine 212 and cysteine 215
Cysteine 280 and cysteine 283 L
Cysteine 212 and cysteine 242
Cysteine 283 and cysteine 305 L
Cysteine 280 and cysteine 305 L
Cysteine 215 and cysteine 242
More...
Cysteine 215 and cysteine 283 L
Cysteine 215 and cysteine 305 L
Cysteine 242 and cysteine 305 L
A redox-regulated disulphide may form between two units of PHD finger protein 6 at cysteines 283 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
87
Peptide A name
PHD finger protein 6
Peptide B name
PHD finger protein 6
Peptide A accession
Q8IWS0
Peptide B accession
Q8IWS0
Peptide A residue number
283
Peptide B residue number
283

Ligandability

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within PHD finger protein 6 between cysteines 292 and 297.

Details

Redox score ?
86
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
7
Peptide accession
Q8IWS0
Residue number A
292
Residue number B
297
Peptide name
PHD finger protein 6

Ligandability

Cysteine 292 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 297 of PHD finger protein 6

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 PHD finger protein 6 between cysteines 297 and 326.

Details

Redox score ?
84
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
4
Peptide accession
Q8IWS0
Residue number A
297
Residue number B
326
Peptide name
PHD finger protein 6

Ligandability

Cysteine 297 of PHD finger protein 6

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 326 of PHD finger protein 6

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 PHD finger protein 6 between cysteines 292 and 326.

Details

Redox score ?
84
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
10
Peptide accession
Q8IWS0
Residue number A
292
Residue number B
326
Peptide name
PHD finger protein 6

Ligandability

Cysteine 292 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 326 of PHD finger protein 6

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 PHD finger protein 6 between cysteines 212 and 215.

Details

Redox score ?
77
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
6
% buried
nan
Peptide accession
Q8IWS0
Residue number A
212
Residue number B
215
Peptide name
PHD finger protein 6

Ligandability

Cysteine 212 of PHD finger protein 6

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 215 of PHD finger protein 6

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 PHD finger protein 6 between cysteines 280 and 283.

Details

Redox score ?
74
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
nan
Peptide accession
Q8IWS0
Residue number A
280
Residue number B
283
Peptide name
PHD finger protein 6

Ligandability

Cysteine 280 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 283 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within PHD finger protein 6 between cysteines 212 and 242.

Details

Redox score ?
74
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
6
% buried
100
Peptide accession
Q8IWS0
Residue number A
212
Residue number B
242
Peptide name
PHD finger protein 6

Ligandability

Cysteine 212 of PHD finger protein 6

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 242 of PHD finger protein 6

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 PHD finger protein 6 between cysteines 283 and 305.

Details

Redox score ?
66
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
93
Peptide accession
Q8IWS0
Residue number A
283
Residue number B
305
Peptide name
PHD finger protein 6

Ligandability

Cysteine 283 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 305 of PHD finger protein 6

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.

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 PHD finger protein 6 between cysteines 280 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
19
% buried
nan
Peptide accession
Q8IWS0
Residue number A
280
Residue number B
305
Peptide name
PHD finger protein 6

Ligandability

Cysteine 280 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 305 of PHD finger protein 6

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.

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 PHD finger protein 6 between cysteines 215 and 242. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
19
% buried
nan
Peptide accession
Q8IWS0
Residue number A
215
Residue number B
242
Peptide name
PHD finger protein 6

Ligandability

Cysteine 215 of PHD finger protein 6

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 242 of PHD finger protein 6

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 PHD finger protein 6 between cysteines 215 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
nan
Peptide accession
Q8IWS0
Residue number A
215
Residue number B
283
Peptide name
PHD finger protein 6

Ligandability

Cysteine 215 of PHD finger protein 6

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 283 of PHD finger protein 6

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within PHD finger protein 6 between cysteines 215 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
19
% buried
nan
Peptide accession
Q8IWS0
Residue number A
215
Residue number B
305
Peptide name
PHD finger protein 6

Ligandability

Cysteine 215 of PHD finger protein 6

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 305 of PHD finger protein 6

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.

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 PHD finger protein 6 between cysteines 242 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
15
PDB code
4nn2
Structure name
protein crystal structure of human borjeson-forssman-lehmann syndrome associated protein phf6
Structure deposition date
2013-11-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
19
% buried
98
Peptide accession
Q8IWS0
Residue number A
242
Residue number B
305
Peptide name
PHD finger protein 6

Ligandability

Cysteine 242 of PHD finger protein 6

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 305 of PHD finger protein 6

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.

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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