NAD-dependent protein deacetylase sirtuin-1
Intermolecular
Cysteine 380 and cysteine 380
Intramolecular
Cysteine 371 and cysteine 374
Cysteine 371 and cysteine 395
Cysteine 371 and cysteine 398
Cysteine 395 and cysteine 398
Cysteine 374 and cysteine 398
Cysteine 374 and cysteine 395
Cysteine 490 and cysteine 501
Cysteine 326 and cysteine 482
Cysteine 501 and cysteine 502
More...Cysteine 490 and cysteine 502
Cysteine 268 and cysteine 482 L
Cysteine 268 and cysteine 326 L
Cysteine 326 and cysteine 501
Cysteine 326 and cysteine 490
Cysteine 326 and cysteine 502
4i5i A 380 B 380
A redox-regulated disulphide may form between two units of NAD-dependent protein deacetylase sirtuin-1 at cysteines 380 and 380.
Details
Redox score ?
76
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
82
Peptide A name
NAD-dependent protein deacetylase sirtuin-1
Peptide B name
NAD-dependent protein deacetylase sirtuin-1
Peptide A accession
Q96EB6
Peptide B accession
Q96EB6
Peptide A residue number
380
Peptide B residue number
380
Ligandability
5btr B 371 B 374
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 371 and 374.
Details
Redox score ?
87
PDB code
5btr
Structure name
crystal structure of sirt1 in complex with resveratrol and an amc- containing peptide
Structure deposition date
2015-06-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
4
Peptide accession
Q96EB6
Residue number A
371
Residue number B
374
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 371 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 374 of NAD-dependent protein deacetylase sirtuin-1
4ig9 G 371 G 395
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 371 and 395.
Details
Redox score ?
86
PDB code
4ig9
Structure name
structure of nad-dependent protein deacetylase sirtuin-1 (open state, 2
Structure deposition date
2012-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
5
Peptide accession
Q96EB6
Residue number A
371
Residue number B
395
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 371 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 395 of NAD-dependent protein deacetylase sirtuin-1
5btr A 371 A 398
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 371 and 398.
Details
Redox score ?
84
PDB code
5btr
Structure name
crystal structure of sirt1 in complex with resveratrol and an amc- containing peptide
Structure deposition date
2015-06-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
6
Peptide accession
Q96EB6
Residue number A
371
Residue number B
398
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 371 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 398 of NAD-dependent protein deacetylase sirtuin-1
5btr B 395 B 398
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 395 and 398.
Details
Redox score ?
82
PDB code
5btr
Structure name
crystal structure of sirt1 in complex with resveratrol and an amc- containing peptide
Structure deposition date
2015-06-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
0
Peptide accession
Q96EB6
Residue number A
395
Residue number B
398
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 395 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 398 of NAD-dependent protein deacetylase sirtuin-1
4ig9 G 374 G 398
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 374 and 398.
Details
Redox score ?
81
PDB code
4ig9
Structure name
structure of nad-dependent protein deacetylase sirtuin-1 (open state, 2
Structure deposition date
2012-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q96EB6
Residue number A
374
Residue number B
398
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 374 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 398 of NAD-dependent protein deacetylase sirtuin-1
4i5i A 374 A 395
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 374 and 395.
Details
Redox score ?
79
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
34
Peptide accession
Q96EB6
Residue number A
374
Residue number B
395
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 374 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 395 of NAD-dependent protein deacetylase sirtuin-1
4if6 A 490 A 501
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 490 and 501.
Details
Redox score ?
71
PDB code
4if6
Structure name
structure of nad-dependent protein deacetylase sirtuin-1 (closed state, 2
Structure deposition date
2012-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
46
Peptide accession
Q96EB6
Residue number A
490
Residue number B
501
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 490 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 501 of NAD-dependent protein deacetylase sirtuin-1
4i5i A 326 A 482
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 326 and 482.
Details
Redox score ?
68
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
100
Peptide accession
Q96EB6
Residue number A
326
Residue number B
482
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 326 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 482 of NAD-dependent protein deacetylase sirtuin-1
4ig9 G 501 G 502
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 501 and 502.
Details
Redox score ?
65
PDB code
4ig9
Structure name
structure of nad-dependent protein deacetylase sirtuin-1 (open state, 2
Structure deposition date
2012-12-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
4
Peptide accession
Q96EB6
Residue number A
501
Residue number B
502
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 501 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 502 of NAD-dependent protein deacetylase sirtuin-1
4i5i B 490 B 502
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 490 and 502. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
36
Peptide accession
Q96EB6
Residue number A
490
Residue number B
502
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 490 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 502 of NAD-dependent protein deacetylase sirtuin-1
4i5i B 268 B 482
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 268 and 482. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
88
Peptide accession
Q96EB6
Residue number A
268
Residue number B
482
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 268 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 482 of NAD-dependent protein deacetylase sirtuin-1
4kxq A 268 A 326
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 268 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4kxq
Structure name
structure of nad-dependent protein deacetylase sirtuin-1 (closed state, 1
Structure deposition date
2013-05-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
78
Peptide accession
Q96EB6
Residue number A
268
Residue number B
326
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 268 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 326 of NAD-dependent protein deacetylase sirtuin-1
4kxq A 326 A 501
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 326 and 501. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4kxq
Structure name
structure of nad-dependent protein deacetylase sirtuin-1 (closed state, 1
Structure deposition date
2013-05-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
66
Peptide accession
Q96EB6
Residue number A
326
Residue number B
501
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 326 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 501 of NAD-dependent protein deacetylase sirtuin-1
4i5i B 326 B 490
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 326 and 490. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
78
Peptide accession
Q96EB6
Residue number A
326
Residue number B
490
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 326 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 490 of NAD-dependent protein deacetylase sirtuin-1
4i5i A 326 A 502
A redox-regulated disulphide may form within NAD-dependent protein deacetylase sirtuin-1 between cysteines 326 and 502. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
4i5i
Structure name
crystal structure of the sirt1 catalytic domain bound to nad and an ex527 analog
Structure deposition date
2012-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
58
Peptide accession
Q96EB6
Residue number A
326
Residue number B
502
Peptide name
NAD-dependent protein deacetylase sirtuin-1
Ligandability
Cysteine 326 of NAD-dependent protein deacetylase sirtuin-1
Cysteine 502 of NAD-dependent protein deacetylase sirtuin-1
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