ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Zinc finger HIT domain-containing protein 3

Intermolecular
Cysteine 143 and cysteine 473 of FMR1-interacting protein NUFIP1
Intramolecular
Cysteine 142 and cysteine 143
A redox-regulated disulphide may form between cysteine 143 of Zinc finger HIT domain-containing protein 3 and cysteine 473 of FMR1-interacting protein NUFIP1.

Details

Redox score ?
72
PDB code
5l85
Structure name
solution structure of the complex between human znhit3 and nufip1 proteins
Structure deposition date
2016-06-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
90
Peptide A name
Zinc finger HIT domain-containing protein 3
Peptide B name
FMR1-interacting protein NUFIP1
Peptide A accession
Q15649
Peptide B accession
Q9UHK0
Peptide A residue number
143
Peptide B residue number
473

Ligandability

Cysteine 143 of Zinc finger HIT domain-containing protein 3

Cysteine 473 of FMR1-interacting protein NUFIP1

A redox-regulated disulphide may form within Zinc finger HIT domain-containing protein 3 between cysteines 142 and 143. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5l85
Structure name
solution structure of the complex between human znhit3 and nufip1 proteins
Structure deposition date
2016-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
54
Peptide accession
Q15649
Residue number A
142
Residue number B
143
Peptide name
Zinc finger HIT domain-containing protein 3

Ligandability

Cysteine 142 of Zinc finger HIT domain-containing protein 3

Cysteine 143 of Zinc finger HIT domain-containing protein 3

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