ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Cystatin-C

Intramolecular
Cysteine 123 and cysteine 143
Cysteine 99 and cysteine 109
Cysteine 69 and cysteine 123
Cysteine 47 and cysteine 123
A redox-regulated disulphide may form within Cystatin-C between cysteines 123 and 143 (97 and 117 respectively in this structure).

Details

Redox score ?
90
PDB code
1g96
Structure name
human cystatin c; dimeric form with 3d domain swapping
Structure deposition date
2000-11-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01034
Residue number A
123
Residue number B
143
Peptide name
Cystatin-C

Ligandability

Cysteine 123 of Cystatin-C

Cysteine 143 of Cystatin-C

A redox-regulated disulphide may form within Cystatin-C between cysteines 99 and 109 (73 and 83 respectively in this structure).

Details

Redox score ?
87
PDB code
1tij
Structure name
3d domain-swapped human cystatin c with amyloid-like intermolecular beta-sheets
Structure deposition date
2004-06-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01034
Residue number A
99
Residue number B
109
Peptide name
Cystatin-C

Ligandability

Cysteine 99 of Cystatin-C

Cysteine 109 of Cystatin-C

A redox-regulated disulphide may form within Cystatin-C between cysteines 69 and 123 (69 and 97 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3gax
Structure name
crystal structure of monomeric human cystatin c stabilized against aggregation
Structure deposition date
2009-02-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01034
Residue number A
69
Residue number B
123
Peptide name
Cystatin-C

Ligandability

Cysteine 69 of Cystatin-C

Cysteine 123 of Cystatin-C

Cysteine 69 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Cystatin-C between cysteines 47 and 123 (47 and 97 respectively in this structure).

Details

Redox score ?
nan
PDB code
3gax
Structure name
crystal structure of monomeric human cystatin c stabilized against aggregation
Structure deposition date
2009-02-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01034
Residue number A
47
Residue number B
123
Peptide name
Cystatin-C

Ligandability

Cysteine 47 of Cystatin-C

Cysteine 123 of Cystatin-C

Cysteine 47 in protein A could not be asigned to a Uniprot residue.
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