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a tool for identifying drug-targetable redox-active disulphides

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Sphingomyelin phosphodiesterase

Intramolecular
Cysteine 582 and cysteine 586
Cysteine 122 and cysteine 133
Cysteine 91 and cysteine 167
Cysteine 592 and cysteine 605
Cysteine 223 and cysteine 228
Cysteine 383 and cysteine 429
Cysteine 94 and cysteine 159
Cysteine 229 and cysteine 252
Cysteine 159 and cysteine 167
Cysteine 94 and cysteine 167
More...
Cysteine 224 and cysteine 248
Cysteine 91 and cysteine 159
Cysteine 223 and cysteine 252
Cysteine 224 and cysteine 225
Cysteine 223 and cysteine 229
Cysteine 91 and cysteine 94
Cysteine 90 and cysteine 118
Cysteine 90 and cysteine 129
A redox-regulated disulphide may form within Sphingomyelin phosphodiesterase between cysteines 582 and 586.

Details

Redox score ?
87
PDB code
5hqn
Structure name
catalytic domain of murine acid sphingomyelinase (asmase, asm, smpd1)
Structure deposition date
2016-01-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
582
Residue number B
586
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 582 of Sphingomyelin phosphodiesterase

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 586 of Sphingomyelin phosphodiesterase

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 between cysteines 122 and 133 (120 and 131 respectively in this structure).

Details

Redox score ?
85
PDB code
5i8r
Structure name
asmase with zinc
Structure deposition date
2016-02-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
122
Residue number B
133
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 122 of Sphingomyelin phosphodiesterase

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 133 of Sphingomyelin phosphodiesterase

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 between cysteines 91 and 167 (89 and 165 respectively in this structure).

Details

Redox score ?
83
PDB code
5jg8
Structure name
crystal structure of human acid sphingomyelinase
Structure deposition date
2016-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
91
Residue number B
167
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 91 of Sphingomyelin phosphodiesterase

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 167 of Sphingomyelin phosphodiesterase

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 between cysteines 592 and 605.

Details

Redox score ?
82
PDB code
5fi9
Structure name
closed form of murine acid sphingomyelinase in complex with bisphosphonate inhibitor abpa
Structure deposition date
2015-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
592
Residue number B
605
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 592 of Sphingomyelin phosphodiesterase

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 605 of Sphingomyelin phosphodiesterase

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 between cysteines 223 and 228 (221 and 226 respectively in this structure).

Details

Redox score ?
81
PDB code
5jg8
Structure name
crystal structure of human acid sphingomyelinase
Structure deposition date
2016-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
223
Residue number B
228
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 223 of Sphingomyelin phosphodiesterase

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 228 of Sphingomyelin phosphodiesterase

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 between cysteines 383 and 429.

Details

Redox score ?
81
PDB code
5fib
Structure name
open form of murine acid sphingomyelinase
Structure deposition date
2015-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
383
Residue number B
429
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 383 of Sphingomyelin phosphodiesterase

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 429 of Sphingomyelin phosphodiesterase

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 between cysteines 94 and 159 (92 and 157 respectively in this structure).

Details

Redox score ?
81
PDB code
5jg8
Structure name
crystal structure of human acid sphingomyelinase
Structure deposition date
2016-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
94
Residue number B
159
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 94 of Sphingomyelin phosphodiesterase

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 159 of Sphingomyelin phosphodiesterase

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 between cysteines 229 and 252 (227 and 250 respectively in this structure).

Details

Redox score ?
80
PDB code
5i85
Structure name
asmase with zinc and phosphocholine
Structure deposition date
2016-02-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
229
Residue number B
252
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 229 of Sphingomyelin phosphodiesterase

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 252 of Sphingomyelin phosphodiesterase

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 between cysteines 159 and 167 (157 and 165 respectively in this structure).

Details

Redox score ?
69
PDB code
5i81
Structure name
asmase with zinc
Structure deposition date
2016-02-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
159
Residue number B
167
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 159 of Sphingomyelin phosphodiesterase

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 167 of Sphingomyelin phosphodiesterase

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 between cysteines 94 and 167 (92 and 165 respectively in this structure).

Details

Redox score ?
68
PDB code
5i8r
Structure name
asmase with zinc
Structure deposition date
2016-02-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
94
Residue number B
167
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 94 of Sphingomyelin phosphodiesterase

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 167 of Sphingomyelin phosphodiesterase

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 between cysteines 224 and 248.

Details

Redox score ?
60
PDB code
5fic
Structure name
open form of murine acid sphingomyelinase in presence of lipid
Structure deposition date
2015-12-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
224
Residue number B
248
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 224 of Sphingomyelin phosphodiesterase

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 248 of Sphingomyelin phosphodiesterase

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 between cysteines 91 and 159 (89 and 157 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
5i81
Structure name
asmase with zinc
Structure deposition date
2016-02-18
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
91
Residue number B
159
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 91 of Sphingomyelin phosphodiesterase

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 159 of Sphingomyelin phosphodiesterase

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 between cysteines 223 and 252 (221 and 250 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
5i8r
Structure name
asmase with zinc
Structure deposition date
2016-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
223
Residue number B
252
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 223 of Sphingomyelin phosphodiesterase

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 252 of Sphingomyelin phosphodiesterase

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 between cysteines 224 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
5fic
Structure name
open form of murine acid sphingomyelinase in presence of lipid
Structure deposition date
2015-12-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
224
Residue number B
225
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 224 of Sphingomyelin phosphodiesterase

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 225 of Sphingomyelin phosphodiesterase

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 between cysteines 223 and 229 (221 and 227 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5i8r
Structure name
asmase with zinc
Structure deposition date
2016-02-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
223
Residue number B
229
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 223 of Sphingomyelin phosphodiesterase

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 229 of Sphingomyelin phosphodiesterase

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 between cysteines 91 and 94 (89 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5jg8
Structure name
crystal structure of human acid sphingomyelinase
Structure deposition date
2016-04-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17405
Residue number A
91
Residue number B
94
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 91 of Sphingomyelin phosphodiesterase

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 94 of Sphingomyelin phosphodiesterase

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 between cysteines 90 and 118. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5fi9
Structure name
closed form of murine acid sphingomyelinase in complex with bisphosphonate inhibitor abpa
Structure deposition date
2015-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
90
Residue number B
118
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 90 of Sphingomyelin phosphodiesterase

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 118 of Sphingomyelin phosphodiesterase

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 between cysteines 90 and 129. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5fi9
Structure name
closed form of murine acid sphingomyelinase in complex with bisphosphonate inhibitor abpa
Structure deposition date
2015-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04519
Residue number A
90
Residue number B
129
Peptide name
Sphingomyelin phosphodiesterase

Ligandability

Cysteine 90 of Sphingomyelin phosphodiesterase

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 129 of Sphingomyelin phosphodiesterase

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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