ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bromodomain PHD finger transcription factor

Intramolecular
Cysteine 387 and cysteine 400
A redox-regulated disulphide may form within Bromodomain PHD finger transcription factor between cysteines 387 and 400 (144 and 157 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6lu5
Structure name
crystal structure of bptf-brd with ligand dcbpin5 bound
Structure deposition date
2020-01-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
50
Peptide accession
J3QQQ8
Residue number A
387
Residue number B
400
Peptide name
Bromodomain PHD finger transcription factor

Ligandability

Cysteine 387 of Bromodomain PHD finger transcription factor

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 400 of Bromodomain PHD finger transcription factor

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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