a tool for identifying drug-targetable redox-active disulphides

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Intramolecular

Cysteine 222 and cysteine 224

A redox-regulated disulphide may form within N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D between cysteines 222 and 224. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

59

PDB code

Structure name

structure of human nape-pld

Structure deposition date

2014-06-17

Thiol separation (Å)

6

Half-sphere exposure sum ?

59

Minimum pK_a ?

12

% buried

81

Peptide accession

Residue number A

222

Residue number B

224

Peptide name

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Ligandability

Cysteine 222 of N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

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 224 of N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

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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