ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein S100-A11

Intermolecular
Cysteine 13 and cysteine 13 L
Cysteine 91 and cysteine 13 L
A redox-regulated disulphide may form between two units of Protein S100-A11 at cysteines 13 and 13.

Details

Redox score ?
63
PDB code
2luc
Structure name
solution structure of human s100 calcium-binding protein a11
Structure deposition date
2012-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
82
Peptide A name
Protein S100-A11
Peptide B name
Protein S100-A11
Peptide A accession
P31949
Peptide B accession
P31949
Peptide A residue number
13
Peptide B residue number
13

Ligandability

A redox-regulated disulphide may form between two units of Protein S100-A11 at cysteines 91 and 13. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2luc
Structure name
solution structure of human s100 calcium-binding protein a11
Structure deposition date
2012-06-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
73
Peptide A name
Protein S100-A11
Peptide B name
Protein S100-A11
Peptide A accession
P31949
Peptide B accession
P31949
Peptide A residue number
91
Peptide B residue number
13

Ligandability

Cysteine 91 of Protein S100-A11

Cysteine 13 of Protein S100-A11

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