ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pygopus homolog 1

Intermolecular
Cysteine 346 and cysteine 346
Cysteine 371 and cysteine 371
Intramolecular
Cysteine 343 and cysteine 346
Cysteine 359 and cysteine 363
Cysteine 343 and cysteine 371
Cysteine 359 and cysteine 395
Cysteine 359 and cysteine 392
Cysteine 361 and cysteine 393
Cysteine 392 and cysteine 395
Cysteine 346 and cysteine 371
More...
Cysteine 363 and cysteine 392
Cysteine 341 and cysteine 390
A redox-regulated disulphide may form between two units of Pygopus homolog 1 at cysteines 346 and 346.

Details

Redox score ?
69
PDB code
2vpe
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
54
Peptide A name
Pygopus homolog 1
Peptide B name
Pygopus homolog 1
Peptide A accession
Q9Y3Y4
Peptide B accession
Q9Y3Y4
Peptide A residue number
346
Peptide B residue number
346

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.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Pygopus homolog 1 at cysteines 371 and 371. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2vpe
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
18
% buried
70
Peptide A name
Pygopus homolog 1
Peptide B name
Pygopus homolog 1
Peptide A accession
Q9Y3Y4
Peptide B accession
Q9Y3Y4
Peptide A residue number
371
Peptide B residue number
371

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.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Pygopus homolog 1 between cysteines 343 and 346.

Details

Redox score ?
89
PDB code
2vpd
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
6
Peptide accession
Q9Y3Y4
Residue number A
343
Residue number B
346
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 343 of Pygopus homolog 1

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 346 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 359 and 363.

Details

Redox score ?
87
PDB code
2vpd
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
21
Peptide accession
Q9Y3Y4
Residue number A
359
Residue number B
363
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 359 of Pygopus homolog 1

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 Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 343 and 371.

Details

Redox score ?
86
PDB code
2vpd
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
7
Peptide accession
Q9Y3Y4
Residue number A
343
Residue number B
371
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 343 of Pygopus homolog 1

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 371 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 359 and 395.

Details

Redox score ?
86
PDB code
2vpg
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
16
Peptide accession
Q9Y3Y4
Residue number A
359
Residue number B
395
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 359 of Pygopus homolog 1

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 395 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 359 and 392.

Details

Redox score ?
85
PDB code
2vpd
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
5
% buried
26
Peptide accession
Q9Y3Y4
Residue number A
359
Residue number B
392
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 359 of Pygopus homolog 1

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 392 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 361 and 393.

Details

Redox score ?
84
PDB code
2dx8
Structure name
crystal structure analysis of the phd domain of the transcription coactivator pygophus
Structure deposition date
2006-08-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q9D0P5
Residue number A
361
Residue number B
393
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 361 of Pygopus homolog 1

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 393 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 392 and 395.

Details

Redox score ?
79
PDB code
2vpd
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
17
Peptide accession
Q9Y3Y4
Residue number A
392
Residue number B
395
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 392 of Pygopus homolog 1

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 395 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 346 and 371.

Details

Redox score ?
76
PDB code
2vpg
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
61
Peptide accession
Q9Y3Y4
Residue number A
346
Residue number B
371
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 346 of Pygopus homolog 1

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 371 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 363 and 392.

Details

Redox score ?
72
PDB code
2vpe
Structure name
decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
Structure deposition date
2008-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
27
Peptide accession
Q9Y3Y4
Residue number A
363
Residue number B
392
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 363 of Pygopus homolog 1

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 392 of Pygopus homolog 1

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 Pygopus homolog 1 between cysteines 341 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2dx8
Structure name
crystal structure analysis of the phd domain of the transcription coactivator pygophus
Structure deposition date
2006-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
5
% buried
9
Peptide accession
Q9D0P5
Residue number A
341
Residue number B
390
Peptide name
Pygopus homolog 1

Ligandability

Cysteine 341 of Pygopus homolog 1

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 390 of Pygopus homolog 1

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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