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Histone acetyltransferase KAT6A

Intramolecular
Cysteine 281 and cysteine 307
Cysteine 230 and cysteine 233
Cysteine 230 and cysteine 259
Cysteine 230 and cysteine 262
Cysteine 540 and cysteine 560
Cysteine 265 and cysteine 268
Cysteine 265 and cysteine 292
Cysteine 540 and cysteine 543
Cysteine 284 and cysteine 310
Cysteine 307 and cysteine 310
More...
Cysteine 543 and cysteine 560
Cysteine 281 and cysteine 310
Cysteine 268 and cysteine 292
Cysteine 233 and cysteine 262
Cysteine 209 and cysteine 241
Cysteine 284 and cysteine 307
Cysteine 209 and cysteine 212
Cysteine 233 and cysteine 259
Cysteine 212 and cysteine 241
Cysteine 259 and cysteine 262
Cysteine 265 and cysteine 293
Cysteine 292 and cysteine 293
Cysteine 281 and cysteine 284
Cysteine 265 and cysteine 307
Cysteine 590 and cysteine 594
Cysteine 293 and cysteine 307
Cysteine 594 and cysteine 646
Cysteine 281 and cysteine 293
A redox-regulated disulphide may form within Histone acetyltransferase KAT6A between cysteines 281 and 307.

Details

Redox score ?
98
PDB code
4ljn
Structure name
crystal structure of moz double phd finger
Structure deposition date
2013-07-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
0
% buried
48
Peptide accession
Q92794
Residue number A
281
Residue number B
307
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 281 of Histone acetyltransferase KAT6A

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 307 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 230 and 233.

Details

Redox score ?
86
PDB code
4lka
Structure name
crystal structure of moz double phd finger histone h3k9ac complex
Structure deposition date
2013-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
3
% buried
30
Peptide accession
Q92794
Residue number A
230
Residue number B
233
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 230 of Histone acetyltransferase KAT6A

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 233 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 230 and 259.

Details

Redox score ?
86
PDB code
4lk9
Structure name
crystal structure of moz double phd finger histone h3 tail complex
Structure deposition date
2013-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
3
% buried
52
Peptide accession
Q92794
Residue number A
230
Residue number B
259
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 230 of Histone acetyltransferase KAT6A

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 259 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 230 and 262.

Details

Redox score ?
84
PDB code
4llb
Structure name
crystal structure of moz double phd finger histone h3k14ac complex
Structure deposition date
2013-07-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
3
% buried
44
Peptide accession
Q92794
Residue number A
230
Residue number B
262
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 230 of Histone acetyltransferase KAT6A

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 262 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 540 and 560.

Details

Redox score ?
84
PDB code
2rc4
Structure name
crystal structure of the hat domain of the human moz protein
Structure deposition date
2007-09-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
4
% buried
44
Peptide accession
Q92794
Residue number A
540
Residue number B
560
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 540 of Histone acetyltransferase KAT6A

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 560 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 265 and 268.

Details

Redox score ?
83
PDB code
4lk9
Structure name
crystal structure of moz double phd finger histone h3 tail complex
Structure deposition date
2013-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
22
Peptide accession
Q92794
Residue number A
265
Residue number B
268
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 265 of Histone acetyltransferase KAT6A

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 268 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 265 and 292.

Details

Redox score ?
83
PDB code
4lk9
Structure name
crystal structure of moz double phd finger histone h3 tail complex
Structure deposition date
2013-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
24
Peptide accession
Q92794
Residue number A
265
Residue number B
292
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 265 of Histone acetyltransferase KAT6A

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 292 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 540 and 543.

Details

Redox score ?
82
PDB code
2rc4
Structure name
crystal structure of the hat domain of the human moz protein
Structure deposition date
2007-09-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
4
% buried
59
Peptide accession
Q92794
Residue number A
540
Residue number B
543
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 540 of Histone acetyltransferase KAT6A

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 543 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 284 and 310.

Details

Redox score ?
82
PDB code
4ljn
Structure name
crystal structure of moz double phd finger
Structure deposition date
2013-07-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
43
Peptide accession
Q92794
Residue number A
284
Residue number B
310
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 284 of Histone acetyltransferase KAT6A

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 310 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 307 and 310.

Details

Redox score ?
81
PDB code
4lka
Structure name
crystal structure of moz double phd finger histone h3k9ac complex
Structure deposition date
2013-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
52
Peptide accession
Q92794
Residue number A
307
Residue number B
310
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 307 of Histone acetyltransferase KAT6A

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 310 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 543 and 560.

Details

Redox score ?
78
PDB code
2rc4
Structure name
crystal structure of the hat domain of the human moz protein
Structure deposition date
2007-09-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
36
Peptide accession
Q92794
Residue number A
543
Residue number B
560
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 543 of Histone acetyltransferase KAT6A

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 560 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 281 and 310.

Details

Redox score ?
78
PDB code
4lka
Structure name
crystal structure of moz double phd finger histone h3k9ac complex
Structure deposition date
2013-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
nan
Peptide accession
Q92794
Residue number A
281
Residue number B
310
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 281 of Histone acetyltransferase KAT6A

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 310 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 268 and 292.

Details

Redox score ?
78
PDB code
5b77
Structure name
crystal structrue of moz double phd finger in complex with histone h3 propionylation at k14
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
5
Peptide accession
Q92794
Residue number A
268
Residue number B
292
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 268 of Histone acetyltransferase KAT6A

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 292 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 233 and 262.

Details

Redox score ?
77
PDB code
4llb
Structure name
crystal structure of moz double phd finger histone h3k14ac complex
Structure deposition date
2013-07-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
24
Peptide accession
Q92794
Residue number A
233
Residue number B
262
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 233 of Histone acetyltransferase KAT6A

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 262 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 209 and 241.

Details

Redox score ?
76
PDB code
6lsb
Structure name
crystal structure of dpf domain of moz in complex with h3k14bz peptide
Structure deposition date
2020-01-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
51
Peptide accession
Q92794
Residue number A
209
Residue number B
241
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 209 of Histone acetyltransferase KAT6A

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 241 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 284 and 307.

Details

Redox score ?
75
PDB code
4ljn
Structure name
crystal structure of moz double phd finger
Structure deposition date
2013-07-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
54
Peptide accession
Q92794
Residue number A
284
Residue number B
307
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 284 of Histone acetyltransferase KAT6A

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 307 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 209 and 212.

Details

Redox score ?
75
PDB code
6lsb
Structure name
crystal structure of dpf domain of moz in complex with h3k14bz peptide
Structure deposition date
2020-01-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
47
Peptide accession
Q92794
Residue number A
209
Residue number B
212
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 209 of Histone acetyltransferase KAT6A

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 212 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 233 and 259.

Details

Redox score ?
74
PDB code
5b77
Structure name
crystal structrue of moz double phd finger in complex with histone h3 propionylation at k14
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
50
Peptide accession
Q92794
Residue number A
233
Residue number B
259
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 233 of Histone acetyltransferase KAT6A

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 259 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 212 and 241.

Details

Redox score ?
72
PDB code
5b75
Structure name
crystal structure of moz double phd finger in complex with histone h3 butyrylation at k14
Structure deposition date
2016-06-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
34
Peptide accession
Q92794
Residue number A
212
Residue number B
241
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 212 of Histone acetyltransferase KAT6A

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 241 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 259 and 262.

Details

Redox score ?
71
PDB code
4llb
Structure name
crystal structure of moz double phd finger histone h3k14ac complex
Structure deposition date
2013-07-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
46
Peptide accession
Q92794
Residue number A
259
Residue number B
262
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 259 of Histone acetyltransferase KAT6A

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 262 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 265 and 293.

Details

Redox score ?
65
PDB code
4ljn
Structure name
crystal structure of moz double phd finger
Structure deposition date
2013-07-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
24
Peptide accession
Q92794
Residue number A
265
Residue number B
293
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 265 of Histone acetyltransferase KAT6A

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 293 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 292 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4llb
Structure name
crystal structure of moz double phd finger histone h3k14ac complex
Structure deposition date
2013-07-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
11
% buried
26
Peptide accession
Q92794
Residue number A
292
Residue number B
293
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 292 of Histone acetyltransferase KAT6A

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 293 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 281 and 284. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4llb
Structure name
crystal structure of moz double phd finger histone h3k14ac complex
Structure deposition date
2013-07-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
19
% buried
nan
Peptide accession
Q92794
Residue number A
281
Residue number B
284
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 281 of Histone acetyltransferase KAT6A

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 284 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 265 and 307. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2ln0
Structure name
structure of moz
Structure deposition date
2011-12-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
5
% buried
28
Peptide accession
Q92794
Residue number A
265
Residue number B
307
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 265 of Histone acetyltransferase KAT6A

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 307 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 590 and 594. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2rc4
Structure name
crystal structure of the hat domain of the human moz protein
Structure deposition date
2007-09-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
79
Peptide accession
Q92794
Residue number A
590
Residue number B
594
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 590 of Histone acetyltransferase KAT6A

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 594 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 293 and 307. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4lka
Structure name
crystal structure of moz double phd finger histone h3k9ac complex
Structure deposition date
2013-07-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
50
Peptide accession
Q92794
Residue number A
293
Residue number B
307
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 293 of Histone acetyltransferase KAT6A

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 307 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 594 and 646. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2rc4
Structure name
crystal structure of the hat domain of the human moz protein
Structure deposition date
2007-09-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
92
Peptide accession
Q92794
Residue number A
594
Residue number B
646
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 594 of Histone acetyltransferase KAT6A

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 646 of Histone acetyltransferase KAT6A

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 KAT6A between cysteines 281 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5b77
Structure name
crystal structrue of moz double phd finger in complex with histone h3 propionylation at k14
Structure deposition date
2016-06-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
nan
Peptide accession
Q92794
Residue number A
281
Residue number B
293
Peptide name
Histone acetyltransferase KAT6A

Ligandability

Cysteine 281 of Histone acetyltransferase KAT6A

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 293 of Histone acetyltransferase KAT6A

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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