DNA repair protein RAD52 homolog

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of DNA repair protein RAD52 homolog at cysteines 25 and 25. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5jrb

Structure name

rad52(1-212) k102a/k133a/e202a mutant

Structure deposition date

2016-05-06

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

DNA repair protein RAD52 homolog

Peptide B name

DNA repair protein RAD52 homolog

Peptide A accession

P43351

Peptide B accession

P43351

Peptide A residue number

Peptide B residue number

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 two units of DNA repair protein RAD52 homolog at cysteines 208 and 29. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1h2i

Structure name

human rad52 protein, n-terminal domain

Structure deposition date

2002-08-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

DNA repair protein RAD52 homolog

Peptide B name

DNA repair protein RAD52 homolog

Peptide A accession

P43351

Peptide B accession

P43351

Peptide A residue number

208

Peptide B residue number

Ligandability

Cysteine 208 of DNA repair protein RAD52 homolog

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 29 of DNA repair protein RAD52 homolog

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 RAD52 homolog between cysteines 25 and 29. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?