a tool for identifying drug-targetable redox-active disulphides

Igh protein

Intramolecular

Cysteine 41 and cysteine 117

A redox-regulated disulphide may form within Igh protein between cysteines 41 and 117 (22 and 98 respectively in this structure).

Details

Redox score ?

80

PDB code

Structure name

nipah virus attachment (g) glycoprotein ectodomain in complex with nah1

Structure deposition date

2022-02-10

Thiol separation (Å)

2

Half-sphere exposure sum ?

82

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

41

Residue number B

117

Peptide name

Igh protein

Ligandability

Cysteine 41 of Igh protein

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 117 of Igh protein

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.

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