Heat shock factor 2-binding protein

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Heat shock factor 2-binding protein at cysteines 120 and 120.

Details

Redox score ?

PDB code

7ldg

Structure name

crystal structure of the meilb2-brca2 complex

Structure deposition date

2021-01-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Heat shock factor 2-binding protein

Peptide B name

Heat shock factor 2-binding protein

Peptide A accession

O75031

Peptide B accession

O75031

Peptide A residue number

120

Peptide B residue number

120

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 Heat shock factor 2-binding protein at cysteines 128 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7bdx

Structure name

armadillo domain of hsf2bp in complex with brca2 peptide

Structure deposition date

2020-12-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide A name

Heat shock factor 2-binding protein

Peptide B name

Heat shock factor 2-binding protein

Peptide A accession

O75031

Peptide B accession

O75031

Peptide A residue number

128

Peptide B residue number

128

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 within Heat shock factor 2-binding protein between cysteines 120 and 128. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?