ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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histone acetyltransferase

Intramolecular
Cysteine 382 and cysteine 388
Cysteine 406 and cysteine 411
Cysteine 382 and cysteine 393
Cysteine 388 and cysteine 393
Cysteine 351 and cysteine 364
Cysteine 364 and cysteine 369
Cysteine 411 and cysteine 414
Cysteine 406 and cysteine 414
Cysteine 351 and cysteine 369
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 382 and 388.

Details

Redox score ?
88
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
4
Peptide accession
Q7Z6C1
Residue number A
382
Residue number B
388
Peptide name
histone acetyltransferase

Ligandability

Cysteine 382 of histone acetyltransferase

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

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 between cysteines 406 and 411.

Details

Redox score ?
86
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
36
Peptide accession
Q7Z6C1
Residue number A
406
Residue number B
411
Peptide name
histone acetyltransferase

Ligandability

Cysteine 406 of histone acetyltransferase

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

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 between cysteines 382 and 393.

Details

Redox score ?
83
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
20
Peptide accession
Q7Z6C1
Residue number A
382
Residue number B
393
Peptide name
histone acetyltransferase

Ligandability

Cysteine 382 of histone acetyltransferase

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

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 between cysteines 388 and 393.

Details

Redox score ?
81
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
22
Peptide accession
Q7Z6C1
Residue number A
388
Residue number B
393
Peptide name
histone acetyltransferase

Ligandability

Cysteine 388 of histone acetyltransferase

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

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 between cysteines 351 and 364.

Details

Redox score ?
80
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
36
Peptide accession
Q7Z6C1
Residue number A
351
Residue number B
364
Peptide name
histone acetyltransferase

Ligandability

Cysteine 351 of histone acetyltransferase

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

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 between cysteines 364 and 369.

Details

Redox score ?
80
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
45
Peptide accession
Q7Z6C1
Residue number A
364
Residue number B
369
Peptide name
histone acetyltransferase

Ligandability

Cysteine 364 of histone acetyltransferase

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 369 of histone acetyltransferase

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 between cysteines 411 and 414.

Details

Redox score ?
80
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
55
Peptide accession
Q7Z6C1
Residue number A
411
Residue number B
414
Peptide name
histone acetyltransferase

Ligandability

Cysteine 411 of histone acetyltransferase

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

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 between cysteines 406 and 414.

Details

Redox score ?
74
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
50
Peptide accession
Q7Z6C1
Residue number A
406
Residue number B
414
Peptide name
histone acetyltransferase

Ligandability

Cysteine 406 of histone acetyltransferase

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

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 between cysteines 351 and 369.

Details

Redox score ?
73
PDB code
7qgs
Structure name
crystal structure of p300 ch1 domain in complex with citif (a cited2- hif-1alpha hybrid)
Structure deposition date
2021-12-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
49
Peptide accession
Q7Z6C1
Residue number A
351
Residue number B
369
Peptide name
histone acetyltransferase

Ligandability

Cysteine 351 of histone acetyltransferase

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 369 of histone acetyltransferase

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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