ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Heterogeneous nuclear ribonucleoprotein L

Intramolecular
Cysteine 264 and cysteine 265
Cysteine 212 and cysteine 215
A redox-regulated disulphide may form within Heterogeneous nuclear ribonucleoprotein L between cysteines 264 and 265 (257 and 258 respectively in this structure).

Details

Redox score ?
63
PDB code
2mqp
Structure name
structural investigation of hnrnp l bound to rna
Structure deposition date
2014-06-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
6
Peptide accession
F2Z3R2
Residue number A
264
Residue number B
265
Peptide name
Heterogeneous nuclear ribonucleoprotein L

Ligandability

Cysteine 264 of Heterogeneous nuclear ribonucleoprotein L

Cysteine 265 of Heterogeneous nuclear ribonucleoprotein L

A redox-regulated disulphide may form within Heterogeneous nuclear ribonucleoprotein L between cysteines 212 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
2mqp
Structure name
structural investigation of hnrnp l bound to rna
Structure deposition date
2014-06-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
58
Peptide accession
F2Z3R2
Residue number A
212
Residue number B
215
Peptide name
Heterogeneous nuclear ribonucleoprotein L

Ligandability

Cysteine 212 of Heterogeneous nuclear ribonucleoprotein L

Cysteine 215 of Heterogeneous nuclear ribonucleoprotein L

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