ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ferritin light chain

Intramolecular
Cysteine 45 and cysteine 49
A redox-regulated disulphide may form within Ferritin light chain between cysteines 45 and 49 (45 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3noz
Structure name
crystal structure of pd(allyl)/apo-e45c/r52h-rhlfr
Structure deposition date
2010-06-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02791
Residue number A
45
Residue number B
49
Peptide name
Ferritin light chain

Ligandability

Cysteine 45 of Ferritin light chain

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.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 49 of Ferritin light chain

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.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 45 in protein A could not be asigned to a Uniprot residue.
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