ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Dihydropyrimidinase

Intramolecular
Cysteine 182 and cysteine 242
Cysteine 126 and cysteine 127
A redox-regulated disulphide may form within Dihydropyrimidinase between cysteines 182 and 242.

Details

Redox score ?
61
PDB code
2vr2
Structure name
human dihydropyrimidinase
Structure deposition date
2008-03-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
Q14117
Residue number A
182
Residue number B
242
Peptide name
Dihydropyrimidinase

Ligandability

Cysteine 182 of Dihydropyrimidinase

Cysteine 242 of Dihydropyrimidinase

A redox-regulated disulphide may form within Dihydropyrimidinase between cysteines 126 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2vr2
Structure name
human dihydropyrimidinase
Structure deposition date
2008-03-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
80
Peptide accession
Q14117
Residue number A
126
Residue number B
127
Peptide name
Dihydropyrimidinase

Ligandability

Cysteine 126 of Dihydropyrimidinase

Cysteine 127 of Dihydropyrimidinase

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