ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Optineurin

Intramolecular
Cysteine 555 and cysteine 575
Cysteine 558 and cysteine 575
Cysteine 555 and cysteine 558
A redox-regulated disulphide may form within Optineurin between cysteines 555 and 575 (498 and 518 respectively in this structure).

Details

Redox score ?
91
PDB code
5aaz
Structure name
tbk1 recruitment to cytosol-invading salmonella induces anti-bacterial autophagy
Structure deposition date
2015-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
Q96CV9
Residue number A
555
Residue number B
575
Peptide name
Optineurin

Ligandability

Cysteine 555 of Optineurin

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 575 of Optineurin

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 Optineurin between cysteines 558 and 575 (501 and 518 respectively in this structure).

Details

Redox score ?
83
PDB code
5aaz
Structure name
tbk1 recruitment to cytosol-invading salmonella induces anti-bacterial autophagy
Structure deposition date
2015-07-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
29
Minimum pKa ?
8
% buried
0
Peptide accession
Q96CV9
Residue number A
558
Residue number B
575
Peptide name
Optineurin

Ligandability

Cysteine 558 of Optineurin

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 575 of Optineurin

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 Optineurin between cysteines 555 and 558 (29 and 32 respectively in this structure).

Details

Redox score ?
80
PDB code
2lo4
Structure name
nmr solution structure of optineurin zinc-finger domain
Structure deposition date
2012-01-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
Q96CV9
Residue number A
555
Residue number B
558
Peptide name
Optineurin

Ligandability

Cysteine 555 of Optineurin

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 558 of Optineurin

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.

If this tool was useful for finding a disulphide, please cite: