ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Non-homologous end-joining factor 1

Intermolecular
Cysteine 202 and cysteine 148
Intramolecular
Cysteine 97 and cysteine 99
Cysteine 99 and cysteine 123
Cysteine 97 and cysteine 123
A redox-regulated disulphide may form between two units of Non-homologous end-joining factor 1 at cysteines 202 and 148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2r9a
Structure name
crystal structure of human xlf
Structure deposition date
2007-09-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
54
Peptide A name
Non-homologous end-joining factor 1
Peptide B name
Non-homologous end-joining factor 1
Peptide A accession
Q9H9Q4
Peptide B accession
Q9H9Q4
Peptide A residue number
202
Peptide B residue number
148

Ligandability

Cysteine 202 of Non-homologous end-joining factor 1

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 148 of Non-homologous end-joining factor 1

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 Non-homologous end-joining factor 1 between cysteines 97 and 99.

Details

Redox score ?
74
PDB code
3rwr
Structure name
crystal structure of the human xrcc4-xlf complex
Structure deposition date
2011-05-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9Q4
Residue number A
97
Residue number B
99
Peptide name
Non-homologous end-joining factor 1

Ligandability

Cysteine 97 of Non-homologous end-joining factor 1

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 99 of Non-homologous end-joining factor 1

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 Non-homologous end-joining factor 1 between cysteines 99 and 123 (599 and 623 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3rwr
Structure name
crystal structure of the human xrcc4-xlf complex
Structure deposition date
2011-05-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9H9Q4
Residue number A
99
Residue number B
123
Peptide name
Non-homologous end-joining factor 1

Ligandability

Cysteine 99 of Non-homologous end-joining factor 1

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 123 of Non-homologous end-joining factor 1

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 Non-homologous end-joining factor 1 between cysteines 97 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3sr2
Structure name
crystal structure of human xlf-xrcc4 complex
Structure deposition date
2011-07-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
54
Peptide accession
Q9H9Q4
Residue number A
97
Residue number B
123
Peptide name
Non-homologous end-joining factor 1

Ligandability

Cysteine 97 of Non-homologous end-joining factor 1

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 123 of Non-homologous end-joining factor 1

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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