ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA excision repair protein ERCC-8

Intermolecular
Cysteine 178 and cysteine 730 of DNA excision repair protein ERCC-6
Intramolecular
Cysteine 171 and cysteine 178
Cysteine 301 and cysteine 303
Cysteine 339 and cysteine 340
Cysteine 252 and cysteine 340
Cysteine 252 and cysteine 301
A redox-regulated disulphide may form between cysteine 178 of DNA excision repair protein ERCC-8 and cysteine 730 of DNA excision repair protein ERCC-6. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
7opc
Structure name
pol ii-csb-crl4csa-uvssa-spt6-paf (structure 4)
Structure deposition date
2021-05-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
86
Peptide A name
DNA excision repair protein ERCC-8
Peptide B name
DNA excision repair protein ERCC-6
Peptide A accession
Q13216
Peptide B accession
Q03468
Peptide A residue number
178
Peptide B residue number
730

Ligandability

Cysteine 178 of DNA excision repair protein ERCC-8

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 730 of DNA excision repair protein ERCC-6

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 DNA excision repair protein ERCC-8 between cysteines 171 and 178.

Details

Redox score ?
77
PDB code
4a11
Structure name
structure of the hsddb1-hscsa complex
Structure deposition date
2011-09-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
45
Peptide accession
Q13216
Residue number A
171
Residue number B
178
Peptide name
DNA excision repair protein ERCC-8

Ligandability

Cysteine 171 of DNA excision repair protein ERCC-8

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 178 of DNA excision repair protein ERCC-8

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 DNA excision repair protein ERCC-8 between cysteines 301 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4a11
Structure name
structure of the hsddb1-hscsa complex
Structure deposition date
2011-09-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
95
Peptide accession
Q13216
Residue number A
301
Residue number B
303
Peptide name
DNA excision repair protein ERCC-8

Ligandability

Cysteine 301 of DNA excision repair protein ERCC-8

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 DNA excision repair protein ERCC-8

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 DNA excision repair protein ERCC-8 between cysteines 339 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4a11
Structure name
structure of the hsddb1-hscsa complex
Structure deposition date
2011-09-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
Q13216
Residue number A
339
Residue number B
340
Peptide name
DNA excision repair protein ERCC-8

Ligandability

Cysteine 339 of DNA excision repair protein ERCC-8

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 340 of DNA excision repair protein ERCC-8

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 DNA excision repair protein ERCC-8 between cysteines 252 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6fcv
Structure name
structure of the human ddb1-csa complex
Structure deposition date
2017-12-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
Q13216
Residue number A
252
Residue number B
340
Peptide name
DNA excision repair protein ERCC-8

Ligandability

Cysteine 252 of DNA excision repair protein ERCC-8

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 340 of DNA excision repair protein ERCC-8

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 DNA excision repair protein ERCC-8 between cysteines 252 and 301. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
6fcv
Structure name
structure of the human ddb1-csa complex
Structure deposition date
2017-12-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
100
Peptide accession
Q13216
Residue number A
252
Residue number B
301
Peptide name
DNA excision repair protein ERCC-8

Ligandability

Cysteine 252 of DNA excision repair protein ERCC-8

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 301 of DNA excision repair protein ERCC-8

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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