ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Intramolecular
Cysteine 280 and cysteine 283 L
Cysteine 259 and cysteine 280 L
Cysteine 256 and cysteine 259
Cysteine 256 and cysteine 283 L
Cysteine 256 and cysteine 280 L
Cysteine 259 and cysteine 283 L
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-3, mitochondrial between cysteines 280 and 283.

Details

Redox score ?
93
PDB code
4bvh
Structure name
crystal structure of human sirt3 in complex with the inhibitor ex-527 and 2'-o-acetyl-adp-ribose
Structure deposition date
2013-06-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
40
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NTG7
Residue number A
280
Residue number B
283
Peptide name
NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Ligandability

Cysteine 280 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 283 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-3, mitochondrial between cysteines 259 and 280.

Details

Redox score ?
93
PDB code
4bvh
Structure name
crystal structure of human sirt3 in complex with the inhibitor ex-527 and 2'-o-acetyl-adp-ribose
Structure deposition date
2013-06-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NTG7
Residue number A
259
Residue number B
280
Peptide name
NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Ligandability

Cysteine 259 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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 280 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-3, mitochondrial between cysteines 256 and 259.

Details

Redox score ?
92
PDB code
4bn5
Structure name
structure of human sirt3 in complex with srt1720 inhibitor
Structure deposition date
2013-05-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NTG7
Residue number A
256
Residue number B
259
Peptide name
NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Ligandability

Cysteine 256 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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 259 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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 NAD-dependent protein deacetylase sirtuin-3, mitochondrial between cysteines 256 and 283.

Details

Redox score ?
92
PDB code
3gls
Structure name
crystal structure of human sirt3
Structure deposition date
2009-03-12
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NTG7
Residue number A
256
Residue number B
283
Peptide name
NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Ligandability

Cysteine 256 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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 283 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-3, mitochondrial between cysteines 256 and 280.

Details

Redox score ?
92
PDB code
4bn5
Structure name
structure of human sirt3 in complex with srt1720 inhibitor
Structure deposition date
2013-05-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
0
Peptide accession
Q9NTG7
Residue number A
256
Residue number B
280
Peptide name
NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Ligandability

Cysteine 256 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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 280 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-3, mitochondrial between cysteines 259 and 283.

Details

Redox score ?
84
PDB code
5h4d
Structure name
crystal structure of hsirt3 in complex with a specific agonist amiodarone hydrochloride
Structure deposition date
2016-10-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NTG7
Residue number A
259
Residue number B
283
Peptide name
NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Ligandability

Cysteine 259 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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 283 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

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