ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Sphingomyelin phosphodiesterase 3

Intramolecular
Cysteine 361 and cysteine 508
Cysteine 361 and cysteine 459
Cysteine 459 and cysteine 508
Cysteine 422 and cysteine 427
A redox-regulated disulphide may form within Sphingomyelin phosphodiesterase 3 between cysteines 361 and 508.

Details

Redox score ?
68
PDB code
5uvg
Structure name
crystal structure of the human neutral sphingomyelinase 2 (nsmase2) catalytic domain with insertion deleted and calcium bound
Structure deposition date
2017-02-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
100
Peptide accession
Q9NY59
Residue number A
361
Residue number B
508
Peptide name
Sphingomyelin phosphodiesterase 3

Ligandability

Cysteine 361 of Sphingomyelin phosphodiesterase 3

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 508 of Sphingomyelin phosphodiesterase 3

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.

A redox-regulated disulphide may form within Sphingomyelin phosphodiesterase 3 between cysteines 361 and 459.

Details

Redox score ?
62
PDB code
5uvg
Structure name
crystal structure of the human neutral sphingomyelinase 2 (nsmase2) catalytic domain with insertion deleted and calcium bound
Structure deposition date
2017-02-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
10
% buried
100
Peptide accession
Q9NY59
Residue number A
361
Residue number B
459
Peptide name
Sphingomyelin phosphodiesterase 3

Ligandability

Cysteine 361 of Sphingomyelin phosphodiesterase 3

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 459 of Sphingomyelin phosphodiesterase 3

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.

A redox-regulated disulphide may form within Sphingomyelin phosphodiesterase 3 between cysteines 459 and 508. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5uvg
Structure name
crystal structure of the human neutral sphingomyelinase 2 (nsmase2) catalytic domain with insertion deleted and calcium bound
Structure deposition date
2017-02-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
100
Peptide accession
Q9NY59
Residue number A
459
Residue number B
508
Peptide name
Sphingomyelin phosphodiesterase 3

Ligandability

Cysteine 459 of Sphingomyelin phosphodiesterase 3

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 508 of Sphingomyelin phosphodiesterase 3

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.

A redox-regulated disulphide may form within Sphingomyelin phosphodiesterase 3 between cysteines 422 and 427. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5uvg
Structure name
crystal structure of the human neutral sphingomyelinase 2 (nsmase2) catalytic domain with insertion deleted and calcium bound
Structure deposition date
2017-02-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
16
Peptide accession
Q9NY59
Residue number A
422
Residue number B
427
Peptide name
Sphingomyelin phosphodiesterase 3

Ligandability

Cysteine 422 of Sphingomyelin phosphodiesterase 3

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 427 of Sphingomyelin phosphodiesterase 3

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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