Transcription factor HES-1

Intermolecular

A redox-regulated disulphide may form between two units of Transcription factor HES-1 at cysteines 128 and 128 (26 and 26 respectively in this structure).

Details

Redox score ?

PDB code

7c4o

Structure name

solution structure of the orange domain from human protein hes1

Structure deposition date

2020-05-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Transcription factor HES-1

Peptide B name

Transcription factor HES-1

Peptide A accession

Q14469

Peptide B accession

Q14469

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 between two units of Transcription factor HES-1 at cysteines 117 and 117 (15 and 15 respectively in this structure).

Details

Redox score ?

PDB code

7c4o

Structure name

solution structure of the orange domain from human protein hes1

Structure deposition date

2020-05-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Transcription factor HES-1

Peptide B name

Transcription factor HES-1

Peptide A accession

Q14469

Peptide B accession

Q14469

Peptide A residue number

117

Peptide B residue number

117

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 Transcription factor HES-1 at cysteines 117 and 146 (15 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?