ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Spermine oxidase

Intramolecular
Cysteine 122 and cysteine 381
Cysteine 207 and cysteine 429
Cysteine 207 and cysteine 409
Cysteine 317 and cysteine 320
Cysteine 409 and cysteine 429
A redox-regulated disulphide may form within Spermine oxidase between cysteines 122 and 381 (102 and 325 respectively in this structure).

Details

Redox score ?
84
PDB code
7oy0
Structure name
structure of human spermine oxidase in complex with a highly selective allosteric inhibitor
Structure deposition date
2021-06-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NWM0
Residue number A
122
Residue number B
381
Peptide name
Spermine oxidase

Ligandability

Cysteine 122 of Spermine oxidase

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 381 of Spermine oxidase

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 Spermine oxidase between cysteines 207 and 429 (187 and 373 respectively in this structure).

Details

Redox score ?
80
PDB code
7oy0
Structure name
structure of human spermine oxidase in complex with a highly selective allosteric inhibitor
Structure deposition date
2021-06-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NWM0
Residue number A
207
Residue number B
429
Peptide name
Spermine oxidase

Ligandability

Cysteine 207 of Spermine oxidase

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 Spermine oxidase

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 Spermine oxidase between cysteines 207 and 409 (187 and 353 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7oxl
Structure name
crystal structure of human spermine oxidase
Structure deposition date
2021-06-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
nan
Peptide accession
Q9NWM0
Residue number A
207
Residue number B
409
Peptide name
Spermine oxidase

Ligandability

Cysteine 207 of Spermine oxidase

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 409 of Spermine oxidase

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 Spermine oxidase between cysteines 317 and 320 (261 and 264 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7oy0
Structure name
structure of human spermine oxidase in complex with a highly selective allosteric inhibitor
Structure deposition date
2021-06-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
22
Peptide accession
Q9NWM0
Residue number A
317
Residue number B
320
Peptide name
Spermine oxidase

Ligandability

Cysteine 317 of Spermine oxidase

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 320 of Spermine oxidase

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 Spermine oxidase between cysteines 409 and 429 (353 and 373 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7oy0
Structure name
structure of human spermine oxidase in complex with a highly selective allosteric inhibitor
Structure deposition date
2021-06-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
nan
Peptide accession
Q9NWM0
Residue number A
409
Residue number B
429
Peptide name
Spermine oxidase

Ligandability

Cysteine 409 of Spermine oxidase

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 Spermine oxidase

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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