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Histone acetyltransferase p300

Intermolecular
Cysteine 1408 and cysteine 1408
Intramolecular
Cysteine 1771 and cysteine 1779
Cysteine 1748 and cysteine 1753
Cysteine 1177 and cysteine 1204
Cysteine 406 and cysteine 411
Cysteine 1796 and cysteine 1801
Cysteine 1247 and cysteine 1250 L
Cysteine 1177 and cysteine 1183
Cysteine 1670 and cysteine 1695
Cysteine 1796 and cysteine 1806
More...
Cysteine 1670 and cysteine 1673
Cysteine 1183 and cysteine 1201
Cysteine 1771 and cysteine 1782
Cysteine 1683 and cysteine 1686
Cysteine 1177 and cysteine 1201
Cysteine 1753 and cysteine 1758
Cysteine 1201 and cysteine 1204
Cysteine 351 and cysteine 364 L
Cysteine 1748 and cysteine 1758
Cysteine 1250 and cysteine 1275 L
Cysteine 1670 and cysteine 1692
Cysteine 1247 and cysteine 1272 L
Cysteine 1692 and cysteine 1695
Cysteine 1779 and cysteine 1782
Cysteine 1673 and cysteine 1692
Cysteine 1183 and cysteine 1204
Cysteine 1250 and cysteine 1272 L
Cysteine 1801 and cysteine 1806
Cysteine 1247 and cysteine 1275 L
Cysteine 1673 and cysteine 1695
Cysteine 1164 and cysteine 1258 L
Cysteine 382 and cysteine 393
Cysteine 1272 and cysteine 1275 L
Cysteine 1163 and cysteine 1164
Cysteine 388 and cysteine 393
Cysteine 364 and cysteine 369 L
Cysteine 382 and cysteine 388
Cysteine 411 and cysteine 414
Cysteine 406 and cysteine 414
Cysteine 1163 and cysteine 1272 L
A redox-regulated disulphide may form between two units of Histone acetyltransferase p300 at cysteines 1408 and 1408.

Details

Redox score ?
80
PDB code
4bhw
Structure name
structural basis for autoinhibition of the acetyltransferase activity of p300
Structure deposition date
2013-04-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
54
Peptide A name
Histone acetyltransferase p300
Peptide B name
Histone acetyltransferase p300
Peptide A accession
Q09472
Peptide B accession
Q09472
Peptide A residue number
1408
Peptide B residue number
1408

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 Histone acetyltransferase p300 between cysteines 1771 and 1779.

Details

Redox score ?
90
PDB code
3io2
Structure name
crystal structure of the taz2 domain of p300
Structure deposition date
2009-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q09472
Residue number A
1771
Residue number B
1779
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1771 of Histone acetyltransferase p300

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 1779 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1748 and 1753 (26 and 31 respectively in this structure).

Details

Redox score ?
89
PDB code
3p57
Structure name
crystal structure of the p300 taz2 domain bound to mef2 on dna
Structure deposition date
2010-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
4
Peptide accession
Q09472
Residue number A
1748
Residue number B
1753
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1748 of Histone acetyltransferase p300

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 1753 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1177 and 1204.

Details

Redox score ?
89
PDB code
7vi0
Structure name
crystal structure of ep300 hat domain in complex with compound 11
Structure deposition date
2021-09-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
4
Peptide accession
Q09472
Residue number A
1177
Residue number B
1204
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1177 of Histone acetyltransferase p300

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 1204 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 406 and 411 (184 and 189 respectively in this structure).

Details

Redox score ?
89
PDB code
1p4q
Structure name
solution structure of the cited2 transactivation domain in complex with the p300 ch1 domain
Structure deposition date
2003-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q09472
Residue number A
406
Residue number B
411
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 406 of Histone acetyltransferase p300

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 411 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1796 and 1801.

Details

Redox score ?
88
PDB code
3io2
Structure name
crystal structure of the taz2 domain of p300
Structure deposition date
2009-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
16
Peptide accession
Q09472
Residue number A
1796
Residue number B
1801
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1796 of Histone acetyltransferase p300

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 1801 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1247 and 1250.

Details

Redox score ?
88
PDB code
5lku
Structure name
crystal structure of the p300 acetyltransferase catalytic core with coenzyme a
Structure deposition date
2016-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
26
Peptide accession
Q09472
Residue number A
1247
Residue number B
1250
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1247 of Histone acetyltransferase p300

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 1250 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1177 and 1183.

Details

Redox score ?
87
PDB code
7vhz
Structure name
crystal structure of ep300 hat domain in complex with compound 7
Structure deposition date
2021-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
9
Peptide accession
Q09472
Residue number A
1177
Residue number B
1183
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1177 of Histone acetyltransferase p300

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 1183 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1670 and 1695 (14 and 39 respectively in this structure).

Details

Redox score ?
87
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
6
Peptide accession
Q09472
Residue number A
1670
Residue number B
1695
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1670 of Histone acetyltransferase p300

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 1695 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1796 and 1806.

Details

Redox score ?
87
PDB code
3io2
Structure name
crystal structure of the taz2 domain of p300
Structure deposition date
2009-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
16
Peptide accession
Q09472
Residue number A
1796
Residue number B
1806
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1796 of Histone acetyltransferase p300

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 1806 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1670 and 1673 (14 and 17 respectively in this structure).

Details

Redox score ?
86
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
6
Peptide accession
Q09472
Residue number A
1670
Residue number B
1673
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1670 of Histone acetyltransferase p300

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 1673 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1183 and 1201.

Details

Redox score ?
86
PDB code
6gyr
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
6
Peptide accession
Q09472
Residue number A
1183
Residue number B
1201
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1183 of Histone acetyltransferase p300

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 1201 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1771 and 1782 (49 and 60 respectively in this structure).

Details

Redox score ?
86
PDB code
3p57
Structure name
crystal structure of the p300 taz2 domain bound to mef2 on dna
Structure deposition date
2010-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
0
Peptide accession
Q09472
Residue number A
1771
Residue number B
1782
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1771 of Histone acetyltransferase p300

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 1782 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1683 and 1686 (27 and 30 respectively in this structure).

Details

Redox score ?
86
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q09472
Residue number A
1683
Residue number B
1686
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1683 of Histone acetyltransferase p300

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 1686 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1177 and 1201.

Details

Redox score ?
85
PDB code
6gyr
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
28
Peptide accession
Q09472
Residue number A
1177
Residue number B
1201
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1177 of Histone acetyltransferase p300

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 1201 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1753 and 1758 (31 and 36 respectively in this structure).

Details

Redox score ?
85
PDB code
3p57
Structure name
crystal structure of the p300 taz2 domain bound to mef2 on dna
Structure deposition date
2010-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
10
Peptide accession
Q09472
Residue number A
1753
Residue number B
1758
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1753 of Histone acetyltransferase p300

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 1758 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1201 and 1204.

Details

Redox score ?
85
PDB code
7vi0
Structure name
crystal structure of ep300 hat domain in complex with compound 11
Structure deposition date
2021-09-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
4
Peptide accession
Q09472
Residue number A
1201
Residue number B
1204
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1201 of Histone acetyltransferase p300

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 1204 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 351 and 364 (129 and 142 respectively in this structure).

Details

Redox score ?
84
PDB code
1p4q
Structure name
solution structure of the cited2 transactivation domain in complex with the p300 ch1 domain
Structure deposition date
2003-04-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
17
Peptide accession
Q09472
Residue number A
351
Residue number B
364
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 351 of Histone acetyltransferase p300

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 364 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1748 and 1758.

Details

Redox score ?
84
PDB code
3io2
Structure name
crystal structure of the taz2 domain of p300
Structure deposition date
2009-08-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
0
Peptide accession
Q09472
Residue number A
1748
Residue number B
1758
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1748 of Histone acetyltransferase p300

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 1758 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1250 and 1275.

Details

Redox score ?
83
PDB code
7vhz
Structure name
crystal structure of ep300 hat domain in complex with compound 7
Structure deposition date
2021-09-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
36
Minimum pKa ?
10
% buried
0
Peptide accession
Q09472
Residue number A
1250
Residue number B
1275
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1250 of Histone acetyltransferase p300

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 1275 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1670 and 1692 (14 and 36 respectively in this structure).

Details

Redox score ?
83
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
6
Peptide accession
Q09472
Residue number A
1670
Residue number B
1692
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1670 of Histone acetyltransferase p300

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 1692 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1247 and 1272.

Details

Redox score ?
82
PDB code
6gyr
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
36
Peptide accession
Q09472
Residue number A
1247
Residue number B
1272
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1247 of Histone acetyltransferase p300

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 1272 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1692 and 1695 (36 and 39 respectively in this structure).

Details

Redox score ?
82
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
0
Peptide accession
Q09472
Residue number A
1692
Residue number B
1695
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1692 of Histone acetyltransferase p300

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 1695 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1779 and 1782 (57 and 60 respectively in this structure).

Details

Redox score ?
81
PDB code
3p57
Structure name
crystal structure of the p300 taz2 domain bound to mef2 on dna
Structure deposition date
2010-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
0
Peptide accession
Q09472
Residue number A
1779
Residue number B
1782
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1779 of Histone acetyltransferase p300

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 1782 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1673 and 1692 (17 and 36 respectively in this structure).

Details

Redox score ?
81
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
0
Peptide accession
Q09472
Residue number A
1673
Residue number B
1692
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1673 of Histone acetyltransferase p300

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 1692 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1183 and 1204.

Details

Redox score ?
81
PDB code
7vhz
Structure name
crystal structure of ep300 hat domain in complex with compound 7
Structure deposition date
2021-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
Q09472
Residue number A
1183
Residue number B
1204
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1183 of Histone acetyltransferase p300

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 1204 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1250 and 1272.

Details

Redox score ?
80
PDB code
7ss8
Structure name
human p300 complexed with a proline-based inhibitor
Structure deposition date
2021-11-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
28
Peptide accession
Q09472
Residue number A
1250
Residue number B
1272
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1250 of Histone acetyltransferase p300

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 1272 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1801 and 1806 (79 and 84 respectively in this structure).

Details

Redox score ?
80
PDB code
3p57
Structure name
crystal structure of the p300 taz2 domain bound to mef2 on dna
Structure deposition date
2010-10-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q09472
Residue number A
1801
Residue number B
1806
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1801 of Histone acetyltransferase p300

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 1806 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1247 and 1275.

Details

Redox score ?
78
PDB code
6gyr
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
24
Peptide accession
Q09472
Residue number A
1247
Residue number B
1275
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1247 of Histone acetyltransferase p300

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 1275 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1673 and 1695 (17 and 39 respectively in this structure).

Details

Redox score ?
78
PDB code
6ds6
Structure name
crystal structure of p300 zz domain in complex with histone h3 peptide
Structure deposition date
2018-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
Q09472
Residue number A
1673
Residue number B
1695
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1673 of Histone acetyltransferase p300

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 1695 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1164 and 1258.

Details

Redox score ?
77
PDB code
6gyr
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
79
Peptide accession
Q09472
Residue number A
1164
Residue number B
1258
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1164 of Histone acetyltransferase p300

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 1258 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 382 and 393 (160 and 171 respectively in this structure).

Details

Redox score ?
77
PDB code
1l3e
Structure name
nmr structures of the hif-1alpha ctad/p300 ch1 complex
Structure deposition date
2002-02-26
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
22
Peptide accession
Q09472
Residue number A
382
Residue number B
393
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 382 of Histone acetyltransferase p300

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 Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1272 and 1275.

Details

Redox score ?
76
PDB code
6gyt
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
38
Peptide accession
Q09472
Residue number A
1272
Residue number B
1275
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1272 of Histone acetyltransferase p300

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 1275 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1163 and 1164.

Details

Redox score ?
75
PDB code
5lkz
Structure name
crystal structure of the p300 acetyltransferase catalytic core with crotonyl-coenzyme a
Structure deposition date
2016-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
66
Peptide accession
Q09472
Residue number A
1163
Residue number B
1164
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1163 of Histone acetyltransferase p300

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 1164 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 388 and 393 (166 and 171 respectively in this structure).

Details

Redox score ?
70
PDB code
1l3e
Structure name
nmr structures of the hif-1alpha ctad/p300 ch1 complex
Structure deposition date
2002-02-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
18
Peptide accession
Q09472
Residue number A
388
Residue number B
393
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 388 of Histone acetyltransferase p300

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 Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 364 and 369 (142 and 147 respectively in this structure).

Details

Redox score ?
66
PDB code
1p4q
Structure name
solution structure of the cited2 transactivation domain in complex with the p300 ch1 domain
Structure deposition date
2003-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
16
% buried
31
Peptide accession
Q09472
Residue number A
364
Residue number B
369
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 364 of Histone acetyltransferase p300

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 369 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 382 and 388 (160 and 166 respectively in this structure).

Details

Redox score ?
66
PDB code
1p4q
Structure name
solution structure of the cited2 transactivation domain in complex with the p300 ch1 domain
Structure deposition date
2003-04-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
19
% buried
0
Peptide accession
Q09472
Residue number A
382
Residue number B
388
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 382 of Histone acetyltransferase p300

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 388 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 411 and 414 (189 and 192 respectively in this structure).

Details

Redox score ?
65
PDB code
1l3e
Structure name
nmr structures of the hif-1alpha ctad/p300 ch1 complex
Structure deposition date
2002-02-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
15
% buried
25
Peptide accession
Q09472
Residue number A
411
Residue number B
414
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 411 of Histone acetyltransferase p300

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 414 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 406 and 414 (184 and 192 respectively in this structure).

Details

Redox score ?
63
PDB code
1l3e
Structure name
nmr structures of the hif-1alpha ctad/p300 ch1 complex
Structure deposition date
2002-02-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
15
% buried
26
Peptide accession
Q09472
Residue number A
406
Residue number B
414
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 406 of Histone acetyltransferase p300

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 414 of Histone acetyltransferase p300

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 Histone acetyltransferase p300 between cysteines 1163 and 1272.

Details

Redox score ?
63
PDB code
6gyr
Structure name
transcription factor dimerization activates the p300 acetyltransferase
Structure deposition date
2018-07-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
1
% buried
56
Peptide accession
Q09472
Residue number A
1163
Residue number B
1272
Peptide name
Histone acetyltransferase p300

Ligandability

Cysteine 1163 of Histone acetyltransferase p300

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 1272 of Histone acetyltransferase p300

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.

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