ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Intramolecular
Cysteine 372 and cysteine 489
Cysteine 395 and cysteine 489
A redox-regulated disulphide may form within Polyribonucleotide nucleotidyltransferase 1, mitochondrial between cysteines 372 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3u1k
Structure name
crystal structure of human pnpase
Structure deposition date
2011-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
92
Minimum pKa ?
10
% buried
80
Peptide accession
Q8TCS8
Residue number A
372
Residue number B
489
Peptide name
Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Ligandability

Cysteine 372 of Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Cysteine 489 of Polyribonucleotide nucleotidyltransferase 1, mitochondrial

A redox-regulated disulphide may form within Polyribonucleotide nucleotidyltransferase 1, mitochondrial between cysteines 395 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3u1k
Structure name
crystal structure of human pnpase
Structure deposition date
2011-09-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
106
Minimum pKa ?
12
% buried
100
Peptide accession
Q8TCS8
Residue number A
395
Residue number B
489
Peptide name
Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Ligandability

Cysteine 395 of Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Cysteine 489 of Polyribonucleotide nucleotidyltransferase 1, mitochondrial

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