a tool for identifying drug-targetable redox-active disulphides

DNA repair protein XRCC4

Intermolecular

Cysteine 130 and cysteine 130

Cysteine 165 and cysteine 165

Cysteine 165 and cysteine 515 of Non-homologous end joining factor IFFO1

Cysteine 165 and cysteine 901 of DNA ligase 4

Intramolecular

Cysteine 128 and cysteine 130

A redox-regulated disulphide may form between two units of DNA repair protein XRCC4 at cysteines 130 and 130 (130 and 630 respectively in this structure).

Details

Redox score ?

77

PDB code

Structure name

crystal structure of the human xrcc4-xlf complex

Structure deposition date

2011-05-09

Thiol separation (Å)

3

Half-sphere exposure sum ?

70

Minimum pK_a ?

nan

% buried

nan

Peptide A name

DNA repair protein XRCC4

Peptide B name

DNA repair protein XRCC4

Peptide A accession

Peptide B accession

Peptide A residue number

130

Peptide B residue number

130

Ligandability

Cysteine 130 of DNA repair protein XRCC4

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 130 of DNA repair protein XRCC4

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 between two units of DNA repair protein XRCC4 at cysteines 165 and 165. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

58

PDB code

Structure name

structure of human xrcc4 in complex with the tandem brct domains of dna ligaseiv

Structure deposition date

2009-07-31

Thiol separation (Å)

6

Half-sphere exposure sum ?

62

Minimum pK_a ?

10

% buried

56

Peptide A name

DNA repair protein XRCC4

Peptide B name

DNA repair protein XRCC4

Peptide A accession

Peptide B accession

Peptide A residue number

165

Peptide B residue number

165

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 between cysteine 165 of DNA repair protein XRCC4 and cysteine 515 of Non-homologous end joining factor IFFO1 (165 and 519 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

Structure name

human xrcc4 and iffo1 complex

Structure deposition date

2018-07-23

Thiol separation (Å)

9

Half-sphere exposure sum ?

37

Minimum pK_a ?

9

% buried

0

Peptide A name

DNA repair protein XRCC4

Peptide B name

Non-homologous end joining factor IFFO1

Peptide A accession

Peptide B accession

Peptide A residue number

165

Peptide B residue number

515

Ligandability

Cysteine 165 of DNA repair protein XRCC4

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 515 of Non-homologous end joining factor IFFO1

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 between cysteine 165 of DNA repair protein XRCC4 and cysteine 901 of DNA ligase 4. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

40

PDB code

Structure name

nhej long-range synaptic complex

Structure deposition date

2021-02-18

Thiol separation (Å)

10

Half-sphere exposure sum ?

57

Minimum pK_a ?

10

% buried

46

Peptide A name

DNA repair protein XRCC4

Peptide B name

DNA ligase 4

Peptide A accession

Peptide B accession

Peptide A residue number

165

Peptide B residue number

901

Ligandability

Cysteine 165 of DNA repair protein XRCC4

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 901 of DNA ligase 4

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 XRCC4 between cysteines 128 and 130. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

crystal structure of the human xrcc4-xlf complex

Structure deposition date

2011-05-09

Thiol separation (Å)

9

Half-sphere exposure sum ?

63

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

128

Residue number B

130

Peptide name

DNA repair protein XRCC4

Ligandability

Cysteine 128 of DNA repair protein XRCC4

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 130 of DNA repair protein XRCC4

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: