ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-glycosylase/DNA lyase

Intramolecular
Cysteine 241 and cysteine 255
Cysteine 28 and cysteine 75
Cysteine 146 and cysteine 163
Cysteine 140 and cysteine 253
Cysteine 140 and cysteine 255
Cysteine 253 and cysteine 255
Cysteine 146 and cysteine 253
A redox-regulated disulphide may form within N-glycosylase/DNA lyase between cysteines 241 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1ebm
Structure name
crystal structure of the human 8-oxoguanine glycosylase (hogg1) bound to a substrate oligonucleotide
Structure deposition date
2000-01-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
78
Peptide accession
O15527
Residue number A
241
Residue number B
255
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 241 of N-glycosylase/DNA lyase

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 255 of N-glycosylase/DNA lyase

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 N-glycosylase/DNA lyase between cysteines 28 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2xhi
Structure name
separation-of-function mutants unravel the dual reaction mode of human 8-oxoguanine dna glycosylase
Structure deposition date
2010-06-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
80
Peptide accession
O15527
Residue number A
28
Residue number B
75
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 28 of N-glycosylase/DNA lyase

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 75 of N-glycosylase/DNA lyase

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 N-glycosylase/DNA lyase between cysteines 146 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6w13
Structure name
human 8-oxoguanine glycosylase interrogating fully intrahelical oxog lesion dna
Structure deposition date
2020-03-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
96
Peptide accession
O15527
Residue number A
146
Residue number B
163
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 146 of N-glycosylase/DNA lyase

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 163 of N-glycosylase/DNA lyase

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 N-glycosylase/DNA lyase between cysteines 140 and 253. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2i5w
Structure name
structure of hogg1 crosslinked to dna sampling a normal g adjacent to an oxog
Structure deposition date
2006-08-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
O15527
Residue number A
140
Residue number B
253
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 140 of N-glycosylase/DNA lyase

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 253 of N-glycosylase/DNA lyase

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 N-glycosylase/DNA lyase between cysteines 140 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3ih7
Structure name
crystal structure of catalytically active human 8-oxoguanine glycosylase distally crosslinked to guanine-containing dna
Structure deposition date
2009-07-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
14
% buried
99
Peptide accession
O15527
Residue number A
140
Residue number B
255
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 140 of N-glycosylase/DNA lyase

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 255 of N-glycosylase/DNA lyase

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 N-glycosylase/DNA lyase between cysteines 253 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
2nof
Structure name
structure of q315f human 8-oxoguanine glycosylase proximal crosslink to 8-oxoguanine dna
Structure deposition date
2006-10-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
11
% buried
94
Peptide accession
O15527
Residue number A
253
Residue number B
255
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 253 of N-glycosylase/DNA lyase

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 255 of N-glycosylase/DNA lyase

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 N-glycosylase/DNA lyase between cysteines 146 and 253 (146 and 207 respectively in this structure).

Details

Redox score ?
nan
PDB code
6w13
Structure name
human 8-oxoguanine glycosylase interrogating fully intrahelical oxog lesion dna
Structure deposition date
2020-03-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
nan
Peptide accession
O15527
Residue number A
146
Residue number B
253
Peptide name
N-glycosylase/DNA lyase

Ligandability

Cysteine 146 of N-glycosylase/DNA lyase

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 253 of N-glycosylase/DNA lyase

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.

Uncertain whether structure cysteine 207 has been assigned to correct residue.
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