ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tubulin alpha chain

Intramolecular
Cysteine 315 and cysteine 347
Cysteine 4 and cysteine 129
Cysteine 295 and cysteine 376
Cysteine 295 and cysteine 315
Cysteine 316 and cysteine 376
Cysteine 315 and cysteine 316
Cysteine 316 and cysteine 347
Cysteine 200 and cysteine 316
A redox-regulated disulphide may form within Tubulin alpha 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 ?
45
PDB code
4drx
Structure name
gtp-tubulin in complex with a darpin
Structure deposition date
2012-02-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
64
Peptide accession
D0VWZ0
Residue number A
315
Residue number B
347
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 315 of Tubulin alpha 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 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 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 ?
41
PDB code
6gvm
Structure name
tubulin:f3ii darpin complex
Structure deposition date
2018-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
76
Peptide accession
D0VWZ0
Residue number A
4
Residue number B
129
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 4 of Tubulin alpha 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 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 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 ?
40
PDB code
4x1i
Structure name
discovery of cytotoxic dolastatin 10 analogs with n-terminal modifications
Structure deposition date
2014-11-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
D0VWZ0
Residue number A
295
Residue number B
376
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 295 of Tubulin alpha 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 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 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 ?
34
PDB code
4x1k
Structure name
discovery of cytotoxic dolastatin 10 analogs with n-terminal modifications
Structure deposition date
2014-11-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
100
Peptide accession
D0VWZ0
Residue number A
295
Residue number B
315
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 295 of Tubulin alpha 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 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 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 ?
30
PDB code
4eb6
Structure name
tubulin-vinblastine: stathmin-like complex
Structure deposition date
2012-03-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
D0VWZ0
Residue number A
316
Residue number B
376
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 316 of Tubulin alpha 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 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 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 ?
30
PDB code
3ryh
Structure name
gmpcpp-tubulin: rb3 stathmin-like domain complex
Structure deposition date
2011-05-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
D0VWZ0
Residue number A
315
Residue number B
316
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 315 of Tubulin alpha 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 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 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 ?
26
PDB code
4x1k
Structure name
discovery of cytotoxic dolastatin 10 analogs with n-terminal modifications
Structure deposition date
2014-11-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
D0VWZ0
Residue number A
316
Residue number B
347
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 316 of Tubulin alpha 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 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 chain between cysteines 200 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
3ryf
Structure name
gtp-tubulin: rb3 stathmin-like domain complex
Structure deposition date
2011-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
D0VWZ0
Residue number A
200
Residue number B
316
Peptide name
Tubulin alpha chain

Ligandability

Cysteine 200 of Tubulin alpha 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 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.

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