Double-strand break repair protein MRE11

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Double-strand break repair protein MRE11 at cysteines 146 and 146.

Details

Redox score ?

PDB code

3t1i

Structure name

crystal structure of human mre11: understanding tumorigenic mutations

Structure deposition date

2011-07-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Double-strand break repair protein MRE11

Peptide B name

Double-strand break repair protein MRE11

Peptide A accession

P49959

Peptide B accession

P49959

Peptide A residue number

146

Peptide B residue number

146

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 Double-strand break repair protein MRE11 at cysteines 146 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

8bah

Structure name

human mre11-nbs1 complex

Structure deposition date

2022-10-11

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Double-strand break repair protein MRE11

Peptide B name

Double-strand break repair protein MRE11

Peptide A accession

P49959

Peptide B accession

P49959

Peptide A residue number

146

Peptide B residue number

Ligandability

Cysteine 146 of Double-strand break repair protein MRE11

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 75 of Double-strand break repair protein MRE11

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 Double-strand break repair protein MRE11 between cysteines 75 and 83. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?