ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Arylamine N-acetyltransferase 2

Intramolecular
Cysteine 223 and cysteine 233
Cysteine 148 and cysteine 151
A redox-regulated disulphide may form within Arylamine N-acetyltransferase 2 between cysteines 223 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2pfr
Structure name
human n-acetyltransferase 2
Structure deposition date
2007-04-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P11245
Residue number A
223
Residue number B
233
Peptide name
Arylamine N-acetyltransferase 2

Ligandability

Cysteine 223 of Arylamine N-acetyltransferase 2

Cysteine 233 of Arylamine N-acetyltransferase 2

A redox-regulated disulphide may form within Arylamine N-acetyltransferase 2 between cysteines 148 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2pfr
Structure name
human n-acetyltransferase 2
Structure deposition date
2007-04-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P11245
Residue number A
148
Residue number B
151
Peptide name
Arylamine N-acetyltransferase 2

Ligandability

Cysteine 148 of Arylamine N-acetyltransferase 2

Cysteine 151 of Arylamine N-acetyltransferase 2

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