ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Adenine DNA glycosylase

Intramolecular
Cysteine 300 and cysteine 307
Cysteine 300 and cysteine 310
Cysteine 294 and cysteine 297
Cysteine 294 and cysteine 303
Cysteine 287 and cysteine 294
Cysteine 287 and cysteine 297
Cysteine 297 and cysteine 303
Cysteine 287 and cysteine 303
Cysteine 336 and cysteine 339
Cysteine 343 and cysteine 397
Cysteine 241 and cysteine 287
A redox-regulated disulphide may form within Adenine DNA glycosylase between cysteines 300 and 307.

Details

Redox score ?
86
PDB code
7ef8
Structure name
crystal structure of mouse mutyh in complex with dna containing ap site analogue:8-oxog (form i)
Structure deposition date
2021-03-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
7
% buried
9
Peptide accession
Q99P21
Residue number A
300
Residue number B
307
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 300 of Adenine DNA glycosylase

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 307 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 300 and 310.

Details

Redox score ?
82
PDB code
7ef8
Structure name
crystal structure of mouse mutyh in complex with dna containing ap site analogue:8-oxog (form i)
Structure deposition date
2021-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
24
Peptide accession
Q99P21
Residue number A
300
Residue number B
310
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 300 of Adenine DNA glycosylase

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 310 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 294 and 297 (283 and 286 respectively in this structure).

Details

Redox score ?
63
PDB code
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
44
Peptide accession
Q9UIF7
Residue number A
294
Residue number B
297
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 294 of Adenine DNA glycosylase

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 297 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 294 and 303 (283 and 292 respectively in this structure).

Details

Redox score ?
61
PDB code
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
38
Peptide accession
Q9UIF7
Residue number A
294
Residue number B
303
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 294 of Adenine DNA glycosylase

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 303 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 287 and 294 (276 and 283 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
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
37
Peptide accession
Q9UIF7
Residue number A
287
Residue number B
294
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 287 of Adenine DNA glycosylase

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 294 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 287 and 297 (276 and 286 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
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
60
Peptide accession
Q9UIF7
Residue number A
287
Residue number B
297
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 287 of Adenine DNA glycosylase

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 297 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 297 and 303 (286 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 ?
58
PDB code
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
61
Peptide accession
Q9UIF7
Residue number A
297
Residue number B
303
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 297 of Adenine DNA glycosylase

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 303 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 287 and 303 (276 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 ?
56
PDB code
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
60
Peptide accession
Q9UIF7
Residue number A
287
Residue number B
303
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 287 of Adenine DNA glycosylase

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 303 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 336 and 339 (325 and 328 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
25
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UIF7
Residue number A
336
Residue number B
339
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 336 of Adenine DNA glycosylase

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 339 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 343 and 397. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7ef9
Structure name
crystal structure of mouse mutyh in complex with dna containing ap site analogue:8-oxog (form ii)
Structure deposition date
2021-03-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
82
Peptide accession
Q99P21
Residue number A
343
Residue number B
397
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 343 of Adenine DNA glycosylase

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 397 of Adenine DNA glycosylase

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 Adenine DNA glycosylase between cysteines 241 and 287 (230 and 276 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3n5n
Structure name
crystal structure analysis of the catalytic domain and interdomain connector of human muty homologue
Structure deposition date
2010-05-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
52
Peptide accession
Q9UIF7
Residue number A
241
Residue number B
287
Peptide name
Adenine DNA glycosylase

Ligandability

Cysteine 241 of Adenine DNA glycosylase

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 287 of Adenine DNA glycosylase

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: