ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Plectin

Intramolecular
Cysteine 850 and cysteine 950
Cysteine 950 and cysteine 992 L
Cysteine 849 and cysteine 950
Cysteine 1119 and cysteine 1122
Cysteine 849 and cysteine 850
Cysteine 850 and cysteine 992 L
Cysteine 848 and cysteine 849
Cysteine 848 and cysteine 850
Cysteine 965 and cysteine 992 L
Cysteine 4454 and cysteine 4494
A redox-regulated disulphide may form within Plectin between cysteines 850 and 950 (740 and 840 respectively in this structure).

Details

Redox score ?
82
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
4
% buried
83
Peptide accession
Q15149
Residue number A
850
Residue number B
950
Peptide name
Plectin

Ligandability

Cysteine 850 of Plectin

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 950 of Plectin

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 Plectin between cysteines 950 and 992 (840 and 882 respectively in this structure).

Details

Redox score ?
78
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
4
% buried
84
Peptide accession
Q15149
Residue number A
950
Residue number B
992
Peptide name
Plectin

Ligandability

Cysteine 950 of Plectin

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 992 of Plectin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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 Plectin between cysteines 849 and 950 (739 and 840 respectively in this structure).

Details

Redox score ?
63
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
53
Peptide accession
Q15149
Residue number A
849
Residue number B
950
Peptide name
Plectin

Ligandability

Cysteine 849 of Plectin

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 950 of Plectin

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 Plectin between cysteines 1119 and 1122 (1009 and 1012 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
5j1i
Structure name
structure of the spectrin repeats 7, 8, and 9 of the plakin domain of plectin
Structure deposition date
2016-03-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
11
Peptide accession
Q15149
Residue number A
1119
Residue number B
1122
Peptide name
Plectin

Ligandability

Cysteine 1119 of Plectin

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 1122 of Plectin

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 Plectin between cysteines 849 and 850 (739 and 740 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
62
Peptide accession
Q15149
Residue number A
849
Residue number B
850
Peptide name
Plectin

Ligandability

Cysteine 849 of Plectin

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 850 of Plectin

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 Plectin between cysteines 850 and 992 (740 and 882 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
14
% buried
92
Peptide accession
Q15149
Residue number A
850
Residue number B
992
Peptide name
Plectin

Ligandability

Cysteine 850 of Plectin

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 992 of Plectin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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 Plectin between cysteines 848 and 849 (738 and 739 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
48
Peptide accession
Q15149
Residue number A
848
Residue number B
849
Peptide name
Plectin

Ligandability

Cysteine 848 of Plectin

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 849 of Plectin

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 Plectin between cysteines 848 and 850 (738 and 740 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
78
Peptide accession
Q15149
Residue number A
848
Residue number B
850
Peptide name
Plectin

Ligandability

Cysteine 848 of Plectin

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 850 of Plectin

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 Plectin between cysteines 965 and 992 (855 and 882 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3pe0
Structure name
structure of the central region of the plakin domain of plectin
Structure deposition date
2010-10-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
63
Peptide accession
Q15149
Residue number A
965
Residue number B
992
Peptide name
Plectin

Ligandability

Cysteine 965 of Plectin

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 992 of Plectin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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 Plectin between cysteines 4454 and 4494. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2n03
Structure name
solution nmr structure plectin repeat domain 6 (4403-4606) of plectin from homo sapiens, northeast structural genomics consortium (nesg) target hr6354e
Structure deposition date
2015-03-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
10
% buried
70
Peptide accession
Q15149
Residue number A
4454
Residue number B
4494
Peptide name
Plectin

Ligandability

Cysteine 4454 of Plectin

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 4494 of Plectin

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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