ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone acetyltransferase KAT8

Intramolecular
Cysteine 210 and cysteine 230
Cysteine 210 and cysteine 213
Cysteine 213 and cysteine 230
Cysteine 260 and cysteine 264
Cysteine 264 and cysteine 316
A redox-regulated disulphide may form within Histone acetyltransferase KAT8 between cysteines 210 and 230 (540 and 560 respectively in this structure).

Details

Redox score ?
92
PDB code
6pd9
Structure name
crystal structure of myst acetyltransferase domain in complex with inhibitor 60
Structure deposition date
2019-06-18
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
3
% buried
46
Peptide accession
Q9H7Z6
Residue number A
210
Residue number B
230
Peptide name
Histone acetyltransferase KAT8

Ligandability

Cysteine 210 of Histone acetyltransferase KAT8

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 230 of Histone acetyltransferase KAT8

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 KAT8 between cysteines 210 and 213.

Details

Redox score ?
83
PDB code
7cmr
Structure name
the crystal structure of human myst1 from biortus
Structure deposition date
2020-07-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
3
% buried
59
Peptide accession
Q9H7Z6
Residue number A
210
Residue number B
213
Peptide name
Histone acetyltransferase KAT8

Ligandability

Cysteine 210 of Histone acetyltransferase KAT8

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 213 of Histone acetyltransferase KAT8

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 KAT8 between cysteines 213 and 230.

Details

Redox score ?
75
PDB code
3qah
Structure name
crystal structure of apo-form human mof catalytic domain
Structure deposition date
2011-01-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
38
Peptide accession
Q9H7Z6
Residue number A
213
Residue number B
230
Peptide name
Histone acetyltransferase KAT8

Ligandability

Cysteine 213 of Histone acetyltransferase KAT8

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 230 of Histone acetyltransferase KAT8

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 KAT8 between cysteines 260 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5j8f
Structure name
human mof k274p crystal structure
Structure deposition date
2016-04-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
61
Peptide accession
Q9H7Z6
Residue number A
260
Residue number B
264
Peptide name
Histone acetyltransferase KAT8

Ligandability

Cysteine 260 of Histone acetyltransferase KAT8

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 264 of Histone acetyltransferase KAT8

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 KAT8 between cysteines 264 and 316 (594 and 646 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6pdd
Structure name
crystal structure of myst acetyltransferase domain in complex with inhibitor 41
Structure deposition date
2019-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
96
Peptide accession
Q9H7Z6
Residue number A
264
Residue number B
316
Peptide name
Histone acetyltransferase KAT8

Ligandability

Cysteine 264 of Histone acetyltransferase KAT8

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 316 of Histone acetyltransferase KAT8

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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