a tool for identifying drug-targetable redox-active disulphides

NACHT, LRR and PYD domains-containing protein 1 allele 2

Intermolecular

Cysteine 866 and cysteine 1013

A redox-regulated disulphide may form between two units of NACHT, LRR and PYD domains-containing protein 1 allele 2 at cysteines 866 and 1013 (85 and 232 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

43

PDB code

Structure name

crystal structure of rnlrp1-fiind

Structure deposition date

2020-08-14

Thiol separation (Å)

8

Half-sphere exposure sum ?

67

Minimum pK_a ?

10

% buried

86

Peptide A name

NACHT, LRR and PYD domains-containing protein 1 allele 2

Peptide B name

NACHT, LRR and PYD domains-containing protein 1 allele 2

Peptide A accession

Peptide B accession

Peptide A residue number

866

Peptide B residue number

1013

Ligandability

Cysteine 866 of NACHT, LRR and PYD domains-containing protein 1 allele 2

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 1013 of NACHT, LRR and PYD domains-containing protein 1 allele 2

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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