ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Protein N-terminal asparagine amidohydrolase

Intramolecular
Cysteine 89 and cysteine 93
Cysteine 75 and cysteine 93
A redox-regulated disulphide may form within Protein N-terminal asparagine amidohydrolase between cysteines 89 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6a0h
Structure name
crystal structure of human protein n-terminal asparagine amidohydrolase (ntan1) c75s mutant with asn-leu-ala-ala-arg peptide
Structure deposition date
2018-06-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
12
% buried
100
Peptide accession
Q96AB6
Residue number A
89
Residue number B
93
Peptide name
Protein N-terminal asparagine amidohydrolase

Ligandability

Cysteine 89 of Protein N-terminal asparagine amidohydrolase

Cysteine 93 of Protein N-terminal asparagine amidohydrolase

A redox-regulated disulphide may form within Protein N-terminal asparagine amidohydrolase between cysteines 75 and 93. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6a0e
Structure name
crystal structure of human protein n-terminal asparagine amidohydrolase (ntan1)
Structure deposition date
2018-06-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
Q96AB6
Residue number A
75
Residue number B
93
Peptide name
Protein N-terminal asparagine amidohydrolase

Ligandability

Cysteine 75 of Protein N-terminal asparagine amidohydrolase

Cysteine 93 of Protein N-terminal asparagine amidohydrolase

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