a tool for identifying drug-targetable redox-active disulphides

NFU1 iron-sulfur cluster scaffold homolog, mitochondrial

Intramolecular

Cysteine 210 and cysteine 213 L

A redox-regulated disulphide may form within NFU1 iron-sulfur cluster scaffold homolog, mitochondrial between cysteines 210 and 213 (60 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

53

PDB code

Structure name

solution nmr structure ctd domain of nfu1 iron-sulfur cluster scaffold homolog from homo sapiens, northeast structural genomics consortium (nesg) target hr2876c

Structure deposition date

2013-03-01

Thiol separation (Å)

9

Half-sphere exposure sum ?

43

Minimum pK_a ?

9

% buried

6

Peptide accession

Residue number A

210

Residue number B

213

Peptide name

NFU1 iron-sulfur cluster scaffold homolog, mitochondrial

Ligandability

Cysteine 210 of NFU1 iron-sulfur cluster scaffold homolog, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 213 of NFU1 iron-sulfur cluster scaffold homolog, mitochondrial

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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