ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Apoptosis-stimulating of p53 protein 2

Intramolecular
Cysteine 1033 and cysteine 1043
Cysteine 1008 and cysteine 1043
Cysteine 968 and cysteine 998
Cysteine 1008 and cysteine 1033
Cysteine 968 and cysteine 1002
Cysteine 28 and cysteine 43
Cysteine 998 and cysteine 1002
Cysteine 35 and cysteine 43
Cysteine 1002 and cysteine 1008
Cysteine 28 and cysteine 35
More...
Cysteine 1002 and cysteine 1043
Cysteine 1002 and cysteine 1033
Cysteine 998 and cysteine 1008
A redox-regulated disulphide may form within Apoptosis-stimulating of p53 protein 2 between cysteines 1033 and 1043.

Details

Redox score ?
85
PDB code
4a63
Structure name
crystal structure of the p73-aspp2 complex at 2
Structure deposition date
2011-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
59
Peptide accession
Q13625
Residue number A
1033
Residue number B
1043
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 1033 of Apoptosis-stimulating of p53 protein 2

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 1043 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 1008 and 1043.

Details

Redox score ?
85
PDB code
4a63
Structure name
crystal structure of the p73-aspp2 complex at 2
Structure deposition date
2011-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
4
% buried
70
Peptide accession
Q13625
Residue number A
1008
Residue number B
1043
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 1008 of Apoptosis-stimulating of p53 protein 2

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 1043 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 968 and 998.

Details

Redox score ?
72
PDB code
6ghm
Structure name
structure of pp1 alpha phosphatase bound to aspp2
Structure deposition date
2018-05-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
76
Peptide accession
Q13625
Residue number A
968
Residue number B
998
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 968 of Apoptosis-stimulating of p53 protein 2

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 998 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 1008 and 1033.

Details

Redox score ?
63
PDB code
6ghm
Structure name
structure of pp1 alpha phosphatase bound to aspp2
Structure deposition date
2018-05-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
9
% buried
68
Peptide accession
Q13625
Residue number A
1008
Residue number B
1033
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 1008 of Apoptosis-stimulating of p53 protein 2

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 1033 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 968 and 1002.

Details

Redox score ?
60
PDB code
4a63
Structure name
crystal structure of the p73-aspp2 complex at 2
Structure deposition date
2011-10-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
46
Peptide accession
Q13625
Residue number A
968
Residue number B
1002
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 968 of Apoptosis-stimulating of p53 protein 2

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 1002 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 28 and 43. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2uwq
Structure name
solution structure of aspp2 n-terminus
Structure deposition date
2007-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
35
Peptide accession
Q13625
Residue number A
28
Residue number B
43
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 28 of Apoptosis-stimulating of p53 protein 2

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 43 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 998 and 1002. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6ghm
Structure name
structure of pp1 alpha phosphatase bound to aspp2
Structure deposition date
2018-05-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
66
Peptide accession
Q13625
Residue number A
998
Residue number B
1002
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 998 of Apoptosis-stimulating of p53 protein 2

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 1002 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 35 and 43. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2uwq
Structure name
solution structure of aspp2 n-terminus
Structure deposition date
2007-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
26
Peptide accession
Q13625
Residue number A
35
Residue number B
43
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 35 of Apoptosis-stimulating of p53 protein 2

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 43 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 1002 and 1008. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4a63
Structure name
crystal structure of the p73-aspp2 complex at 2
Structure deposition date
2011-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
61
Peptide accession
Q13625
Residue number A
1002
Residue number B
1008
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 1002 of Apoptosis-stimulating of p53 protein 2

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 1008 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 28 and 35. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2uwq
Structure name
solution structure of aspp2 n-terminus
Structure deposition date
2007-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
58
Peptide accession
Q13625
Residue number A
28
Residue number B
35
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 28 of Apoptosis-stimulating of p53 protein 2

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 35 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 1002 and 1043. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6ghm
Structure name
structure of pp1 alpha phosphatase bound to aspp2
Structure deposition date
2018-05-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
50
Peptide accession
Q13625
Residue number A
1002
Residue number B
1043
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 1002 of Apoptosis-stimulating of p53 protein 2

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 1043 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 1002 and 1033. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4a63
Structure name
crystal structure of the p73-aspp2 complex at 2
Structure deposition date
2011-10-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
40
Peptide accession
Q13625
Residue number A
1002
Residue number B
1033
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 1002 of Apoptosis-stimulating of p53 protein 2

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 1033 of Apoptosis-stimulating of p53 protein 2

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 Apoptosis-stimulating of p53 protein 2 between cysteines 998 and 1008. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6ghm
Structure name
structure of pp1 alpha phosphatase bound to aspp2
Structure deposition date
2018-05-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
9
% buried
89
Peptide accession
Q13625
Residue number A
998
Residue number B
1008
Peptide name
Apoptosis-stimulating of p53 protein 2

Ligandability

Cysteine 998 of Apoptosis-stimulating of p53 protein 2

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 1008 of Apoptosis-stimulating of p53 protein 2

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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