a tool for identifying drug-targetable redox-active disulphides

Non-homologous end joining factor IFFO1

Intermolecular

Cysteine 165 of DNA repair protein XRCC4 and cysteine 515

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.

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