Histone acetyltransferase KAT6B
Intramolecular
Cysteine 291 and cysteine 317
Cysteine 237 and cysteine 269
Cysteine 291 and cysteine 314
Cysteine 237 and cysteine 240
Cysteine 288 and cysteine 291
Cysteine 216 and cysteine 248
Cysteine 216 and cysteine 219
Cysteine 237 and cysteine 266
Cysteine 314 and cysteine 317
Cysteine 272 and cysteine 275
More...Cysteine 240 and cysteine 269
Cysteine 272 and cysteine 299
Cysteine 288 and cysteine 317
Cysteine 240 and cysteine 266
Cysteine 288 and cysteine 314
Cysteine 219 and cysteine 248
Cysteine 266 and cysteine 269
Cysteine 272 and cysteine 300
Cysteine 275 and cysteine 299
Cysteine 299 and cysteine 300
Cysteine 300 and cysteine 314
Cysteine 288 and cysteine 300
6oie B 291 B 317
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 291 and 317.
Details
Redox score ?
91
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
2
% buried
56
Peptide accession
Q8WYB5
Residue number A
291
Residue number B
317
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 291 of Histone acetyltransferase KAT6B
Cysteine 317 of Histone acetyltransferase KAT6B
6oie B 237 B 269
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 237 and 269.
Details
Redox score ?
89
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
3
% buried
39
Peptide accession
Q8WYB5
Residue number A
237
Residue number B
269
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 237 of Histone acetyltransferase KAT6B
Cysteine 269 of Histone acetyltransferase KAT6B
5u2j B 284 B 307
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 291 and 314 (284 and 307 respectively in this structure).
Details
Redox score ?
88
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
2
% buried
70
Peptide accession
Q8WYB5
Residue number A
291
Residue number B
314
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 291 of Histone acetyltransferase KAT6B
Cysteine 314 of Histone acetyltransferase KAT6B
6oie B 237 B 240
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 237 and 240.
Details
Redox score ?
88
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
3
% buried
34
Peptide accession
Q8WYB5
Residue number A
237
Residue number B
240
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 237 of Histone acetyltransferase KAT6B
Cysteine 240 of Histone acetyltransferase KAT6B
6oie B 288 B 291
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 288 and 291.
Details
Redox score ?
86
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
2
% buried
69
Peptide accession
Q8WYB5
Residue number A
288
Residue number B
291
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 288 of Histone acetyltransferase KAT6B
Cysteine 291 of Histone acetyltransferase KAT6B
5u2j A 209 A 241
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 216 and 248 (209 and 241 respectively in this structure).
Details
Redox score ?
82
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
37
Peptide accession
Q8WYB5
Residue number A
216
Residue number B
248
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 216 of Histone acetyltransferase KAT6B
Cysteine 248 of Histone acetyltransferase KAT6B
5u2j A 209 A 212
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 216 and 219 (209 and 212 respectively in this structure).
Details
Redox score ?
82
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
28
Peptide accession
Q8WYB5
Residue number A
216
Residue number B
219
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 216 of Histone acetyltransferase KAT6B
Cysteine 219 of Histone acetyltransferase KAT6B
5u2j A 230 A 259
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 237 and 266 (230 and 259 respectively in this structure).
Details
Redox score ?
81
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
46
Peptide accession
Q8WYB5
Residue number A
237
Residue number B
266
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 237 of Histone acetyltransferase KAT6B
Cysteine 266 of Histone acetyltransferase KAT6B
5u2j A 307 A 310
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 314 and 317 (307 and 310 respectively in this structure).
Details
Redox score ?
81
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
34
Peptide accession
Q8WYB5
Residue number A
314
Residue number B
317
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 314 of Histone acetyltransferase KAT6B
Cysteine 317 of Histone acetyltransferase KAT6B
5u2j A 265 A 268
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 272 and 275 (265 and 268 respectively in this structure).
Details
Redox score ?
81
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
nan
Peptide accession
Q8WYB5
Residue number A
272
Residue number B
275
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 272 of Histone acetyltransferase KAT6B
Cysteine 275 of Histone acetyltransferase KAT6B
5u2j B 233 B 262
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 240 and 269 (233 and 262 respectively in this structure).
Details
Redox score ?
80
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
20
Peptide accession
Q8WYB5
Residue number A
240
Residue number B
269
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 240 of Histone acetyltransferase KAT6B
Cysteine 269 of Histone acetyltransferase KAT6B
6oie B 272 B 299
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 272 and 299.
Details
Redox score ?
78
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
7
% buried
43
Peptide accession
Q8WYB5
Residue number A
272
Residue number B
299
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 272 of Histone acetyltransferase KAT6B
Cysteine 299 of Histone acetyltransferase KAT6B
5u2j A 281 A 310
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 288 and 317 (281 and 310 respectively in this structure).
Details
Redox score ?
78
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
nan
Peptide accession
Q8WYB5
Residue number A
288
Residue number B
317
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 288 of Histone acetyltransferase KAT6B
Cysteine 317 of Histone acetyltransferase KAT6B
6oie B 240 B 266
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 240 and 266.
Details
Redox score ?
77
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
36
Peptide accession
Q8WYB5
Residue number A
240
Residue number B
266
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 240 of Histone acetyltransferase KAT6B
Cysteine 266 of Histone acetyltransferase KAT6B
6oie B 288 B 314
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 288 and 314.
Details
Redox score ?
76
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
63
Peptide accession
Q8WYB5
Residue number A
288
Residue number B
314
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 288 of Histone acetyltransferase KAT6B
Cysteine 314 of Histone acetyltransferase KAT6B
6oie B 219 B 248
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 219 and 248.
Details
Redox score ?
75
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
22
Peptide accession
Q8WYB5
Residue number A
219
Residue number B
248
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 219 of Histone acetyltransferase KAT6B
Cysteine 248 of Histone acetyltransferase KAT6B
5u2j A 259 A 262
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 266 and 269 (259 and 262 respectively in this structure).
Details
Redox score ?
73
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
38
Peptide accession
Q8WYB5
Residue number A
266
Residue number B
269
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 266 of Histone acetyltransferase KAT6B
Cysteine 269 of Histone acetyltransferase KAT6B
5u2j B 265 B 293
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 272 and 300 (265 and 293 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
52
Peptide accession
Q8WYB5
Residue number A
272
Residue number B
300
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 272 of Histone acetyltransferase KAT6B
Cysteine 300 of Histone acetyltransferase KAT6B
5u2j A 268 A 292
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 275 and 299 (268 and 292 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
19
% buried
nan
Peptide accession
Q8WYB5
Residue number A
275
Residue number B
299
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 275 of Histone acetyltransferase KAT6B
Cysteine 299 of Histone acetyltransferase KAT6B
6oie B 299 B 300
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 299 and 300. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
6oie
Structure name
the double phd finger (dpf) of morf in complex with histone h3k14cr
Structure deposition date
2019-04-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
34
Peptide accession
Q8WYB5
Residue number A
299
Residue number B
300
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 299 of Histone acetyltransferase KAT6B
Cysteine 300 of Histone acetyltransferase KAT6B
5u2j B 293 B 307
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 300 and 314 (293 and 307 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
56
Peptide accession
Q8WYB5
Residue number A
300
Residue number B
314
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 300 of Histone acetyltransferase KAT6B
Cysteine 314 of Histone acetyltransferase KAT6B
5u2j A 281 A 293
A redox-regulated disulphide may form within Histone acetyltransferase KAT6B between cysteines 288 and 300 (281 and 293 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5u2j
Structure name
morf double phd finger (dpf) in complex with histone h3k14bu
Structure deposition date
2016-11-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
nan
Peptide accession
Q8WYB5
Residue number A
288
Residue number B
300
Peptide name
Histone acetyltransferase KAT6B
Ligandability
Cysteine 288 of Histone acetyltransferase KAT6B
Cysteine 300 of Histone acetyltransferase KAT6B
If this tool was useful for finding a disulphide, please cite: