ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cystatin-F

Intramolecular
Cysteine 124 and cysteine 144
Cysteine 99 and cysteine 110
Cysteine 63 and cysteine 144
A redox-regulated disulphide may form within Cystatin-F between cysteines 124 and 144.

Details

Redox score ?
87
PDB code
2ch9
Structure name
crystal structure of dimeric human cystatin f
Structure deposition date
2006-03-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
O76096
Residue number A
124
Residue number B
144
Peptide name
Cystatin-F

Ligandability

Cysteine 124 of Cystatin-F

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 144 of Cystatin-F

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 Cystatin-F between cysteines 99 and 110.

Details

Redox score ?
87
PDB code
2ch9
Structure name
crystal structure of dimeric human cystatin f
Structure deposition date
2006-03-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
O76096
Residue number A
99
Residue number B
110
Peptide name
Cystatin-F

Ligandability

Cysteine 99 of Cystatin-F

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 110 of Cystatin-F

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 Cystatin-F between cysteines 63 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2ch9
Structure name
crystal structure of dimeric human cystatin f
Structure deposition date
2006-03-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
nan
Peptide accession
O76096
Residue number A
63
Residue number B
144
Peptide name
Cystatin-F

Ligandability

Cysteine 63 of Cystatin-F

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 144 of Cystatin-F

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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