ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tubulin alpha-1C chain

Intramolecular
Cysteine 4 and cysteine 129
Cysteine 295 and cysteine 376 L
Cysteine 315 and cysteine 347
Cysteine 316 and cysteine 347 L
Cysteine 295 and cysteine 315
Cysteine 315 and cysteine 316 L
Cysteine 20 and cysteine 25 L
Cysteine 316 and cysteine 376 L
A redox-regulated disulphide may form within Tubulin alpha-1C chain between cysteines 4 and 129. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3e22
Structure name
tubulin-colchicine-soblidotin: stathmin-like domain complex
Structure deposition date
2008-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
72
Peptide accession
Q3ZCJ7
Residue number A
4
Residue number B
129
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 4 of Tubulin alpha-1C chain

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 129 of Tubulin alpha-1C chain

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 Tubulin alpha-1C chain between cysteines 295 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3du7
Structure name
tubulin-colchicine-phomopsin a: stathmin-like domain complex
Structure deposition date
2008-07-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
98
Peptide accession
Q3ZCJ7
Residue number A
295
Residue number B
376
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 295 of Tubulin alpha-1C chain

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 376 of Tubulin alpha-1C chain

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.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tubulin alpha-1C chain between cysteines 315 and 347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3du7
Structure name
tubulin-colchicine-phomopsin a: stathmin-like domain complex
Structure deposition date
2008-07-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
Q3ZCJ7
Residue number A
315
Residue number B
347
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 315 of Tubulin alpha-1C chain

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 347 of Tubulin alpha-1C chain

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 Tubulin alpha-1C chain between cysteines 316 and 347. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3du7
Structure name
tubulin-colchicine-phomopsin a: stathmin-like domain complex
Structure deposition date
2008-07-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
76
Peptide accession
Q3ZCJ7
Residue number A
316
Residue number B
347
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 316 of Tubulin alpha-1C chain

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 347 of Tubulin alpha-1C chain

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 Tubulin alpha-1C chain between cysteines 295 and 315. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3e22
Structure name
tubulin-colchicine-soblidotin: stathmin-like domain complex
Structure deposition date
2008-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
Q3ZCJ7
Residue number A
295
Residue number B
315
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 295 of Tubulin alpha-1C chain

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 315 of Tubulin alpha-1C chain

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 Tubulin alpha-1C chain between cysteines 315 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3du7
Structure name
tubulin-colchicine-phomopsin a: stathmin-like domain complex
Structure deposition date
2008-07-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
Q3ZCJ7
Residue number A
315
Residue number B
316
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 315 of Tubulin alpha-1C chain

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 316 of Tubulin alpha-1C chain

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tubulin alpha-1C chain between cysteines 20 and 25. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3du7
Structure name
tubulin-colchicine-phomopsin a: stathmin-like domain complex
Structure deposition date
2008-07-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
94
Peptide accession
Q3ZCJ7
Residue number A
20
Residue number B
25
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 20 of Tubulin alpha-1C chain

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 25 of Tubulin alpha-1C chain

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 Tubulin alpha-1C chain between cysteines 316 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3e22
Structure name
tubulin-colchicine-soblidotin: stathmin-like domain complex
Structure deposition date
2008-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
Q3ZCJ7
Residue number A
316
Residue number B
376
Peptide name
Tubulin alpha-1C chain

Ligandability

Cysteine 316 of Tubulin alpha-1C chain

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 376 of Tubulin alpha-1C chain

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.

Ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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