ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone acetyltransferase KAT7

Intramolecular
Cysteine 368 and cysteine 388
Cysteine 368 and cysteine 371
Cysteine 371 and cysteine 388
Cysteine 418 and cysteine 422
Cysteine 422 and cysteine 474
A redox-regulated disulphide may form within Histone acetyltransferase KAT7 between cysteines 368 and 388.

Details

Redox score ?
91
PDB code
7d0o
Structure name
crystal structure of human hbo1-brpf2 in apo form
Structure deposition date
2020-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
3
% buried
42
Peptide accession
O95251
Residue number A
368
Residue number B
388
Peptide name
Histone acetyltransferase KAT7

Ligandability

Cysteine 368 of Histone acetyltransferase KAT7

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 KAT7

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 KAT7 between cysteines 368 and 371.

Details

Redox score ?
85
PDB code
7d0o
Structure name
crystal structure of human hbo1-brpf2 in apo form
Structure deposition date
2020-09-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
54
Peptide accession
O95251
Residue number A
368
Residue number B
371
Peptide name
Histone acetyltransferase KAT7

Ligandability

Cysteine 368 of Histone acetyltransferase KAT7

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 371 of Histone acetyltransferase KAT7

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 KAT7 between cysteines 371 and 388.

Details

Redox score ?
77
PDB code
7d0p
Structure name
crystal structure of human hbo1-brpf2 in complex with propionyl- coenzyme a
Structure deposition date
2020-09-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
34
Peptide accession
O95251
Residue number A
371
Residue number B
388
Peptide name
Histone acetyltransferase KAT7

Ligandability

Cysteine 371 of Histone acetyltransferase KAT7

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 KAT7

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 KAT7 between cysteines 418 and 422. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7d0p
Structure name
crystal structure of human hbo1-brpf2 in complex with propionyl- coenzyme a
Structure deposition date
2020-09-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
86
Peptide accession
O95251
Residue number A
418
Residue number B
422
Peptide name
Histone acetyltransferase KAT7

Ligandability

Cysteine 418 of Histone acetyltransferase KAT7

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 422 of Histone acetyltransferase KAT7

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 KAT7 between cysteines 422 and 474. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7d0p
Structure name
crystal structure of human hbo1-brpf2 in complex with propionyl- coenzyme a
Structure deposition date
2020-09-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
96
Peptide accession
O95251
Residue number A
422
Residue number B
474
Peptide name
Histone acetyltransferase KAT7

Ligandability

Cysteine 422 of Histone acetyltransferase KAT7

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 474 of Histone acetyltransferase KAT7

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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