ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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DNA repair protein XRCC1

Intermolecular
Cysteine 12 and cysteine 12
Intramolecular
Cysteine 12 and cysteine 20
Cysteine 12 and cysteine 132 L
A redox-regulated disulphide may form between two units of DNA repair protein XRCC1 at cysteines 12 and 12. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3k77
Structure name
x-ray crystal structure of xrcc1
Structure deposition date
2009-10-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide A name
DNA repair protein XRCC1
Peptide B name
DNA repair protein XRCC1
Peptide A accession
P18887
Peptide B accession
P18887
Peptide A residue number
12
Peptide B residue number
12

Ligandability

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 repair protein XRCC1 between cysteines 12 and 20. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
3k77
Structure name
x-ray crystal structure of xrcc1
Structure deposition date
2009-10-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
28
Peptide accession
P18887
Residue number A
12
Residue number B
20
Peptide name
DNA repair protein XRCC1

Ligandability

Cysteine 12 of DNA repair protein XRCC1

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 20 of DNA repair protein XRCC1

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 repair protein XRCC1 between cysteines 12 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3k77
Structure name
x-ray crystal structure of xrcc1
Structure deposition date
2009-10-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
73
Peptide accession
P18887
Residue number A
12
Residue number B
132
Peptide name
DNA repair protein XRCC1

Ligandability

Cysteine 12 of DNA repair protein XRCC1

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 132 of DNA repair protein XRCC1

Not ligandable in the dataset of Yang et al.

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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