ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

histone acetyltransferase

Intramolecular
Cysteine 397 and cysteine 403
Cysteine 421 and cysteine 426
Cysteine 379 and cysteine 384
Cysteine 426 and cysteine 429
Cysteine 366 and cysteine 379
Cysteine 397 and cysteine 408
Cysteine 421 and cysteine 429
Cysteine 403 and cysteine 408
Cysteine 366 and cysteine 384
A redox-regulated disulphide may form within histone acetyltransferase between cysteines 397 and 403.

Details

Redox score ?
94
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
0
Peptide accession
Q6GQV9
Residue number A
397
Residue number B
403
Peptide name
histone acetyltransferase

Ligandability

Cysteine 397 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 403 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 421 and 426.

Details

Redox score ?
92
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
2
% buried
42
Peptide accession
Q6GQV9
Residue number A
421
Residue number B
426
Peptide name
histone acetyltransferase

Ligandability

Cysteine 421 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 426 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 379 and 384.

Details

Redox score ?
89
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
26
Peptide accession
Q6GQV9
Residue number A
379
Residue number B
384
Peptide name
histone acetyltransferase

Ligandability

Cysteine 379 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 384 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 426 and 429.

Details

Redox score ?
88
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
2
% buried
62
Peptide accession
Q6GQV9
Residue number A
426
Residue number B
429
Peptide name
histone acetyltransferase

Ligandability

Cysteine 426 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 429 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 366 and 379.

Details

Redox score ?
88
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
20
Peptide accession
Q6GQV9
Residue number A
366
Residue number B
379
Peptide name
histone acetyltransferase

Ligandability

Cysteine 366 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 379 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 397 and 408.

Details

Redox score ?
86
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
15
Peptide accession
Q6GQV9
Residue number A
397
Residue number B
408
Peptide name
histone acetyltransferase

Ligandability

Cysteine 397 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 408 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 421 and 429.

Details

Redox score ?
82
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
50
Peptide accession
Q6GQV9
Residue number A
421
Residue number B
429
Peptide name
histone acetyltransferase

Ligandability

Cysteine 421 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 429 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 403 and 408.

Details

Redox score ?
81
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
15
Peptide accession
Q6GQV9
Residue number A
403
Residue number B
408
Peptide name
histone acetyltransferase

Ligandability

Cysteine 403 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 408 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 366 and 384.

Details

Redox score ?
81
PDB code
2ka4
Structure name
nmr structure of the cbp-taz1/stat2-tad complex
Structure deposition date
2008-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
31
Peptide accession
Q6GQV9
Residue number A
366
Residue number B
384
Peptide name
histone acetyltransferase

Ligandability

Cysteine 366 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 384 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.

If this tool was useful for finding a disulphide, please cite: