ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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SEC14-like protein 3

Intramolecular
Cysteine 301 and cysteine 355
Cysteine 89 and cysteine 254
Cysteine 96 and cysteine 135
A redox-regulated disulphide may form within SEC14-like protein 3 between cysteines 301 and 355.

Details

Redox score ?
78
PDB code
4uyb
Structure name
crystal structure of sec14-like protein 3
Structure deposition date
2014-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
50
Peptide accession
Q9UDX4
Residue number A
301
Residue number B
355
Peptide name
SEC14-like protein 3

Ligandability

Cysteine 301 of SEC14-like protein 3

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 355 of SEC14-like protein 3

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 SEC14-like protein 3 between cysteines 89 and 254.

Details

Redox score ?
66
PDB code
4uyb
Structure name
crystal structure of sec14-like protein 3
Structure deposition date
2014-08-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
50
Peptide accession
Q9UDX4
Residue number A
89
Residue number B
254
Peptide name
SEC14-like protein 3

Ligandability

Cysteine 89 of SEC14-like protein 3

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 254 of SEC14-like protein 3

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 SEC14-like protein 3 between cysteines 96 and 135. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4uyb
Structure name
crystal structure of sec14-like protein 3
Structure deposition date
2014-08-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
74
Peptide accession
Q9UDX4
Residue number A
96
Residue number B
135
Peptide name
SEC14-like protein 3

Ligandability

Cysteine 96 of SEC14-like protein 3

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 135 of SEC14-like protein 3

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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