ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tubulin alpha-1A chain

Intramolecular
Cysteine 315 and cysteine 316 L
Cysteine 4 and cysteine 129 L
Cysteine 316 and cysteine 347 L
Cysteine 295 and cysteine 376 L
Cysteine 295 and cysteine 315
Cysteine 315 and cysteine 347 L
Cysteine 316 and cysteine 376 L
Cysteine 20 and cysteine 25 L
Cysteine 200 and cysteine 316 L
Cysteine 4 and cysteine 20 L
Cysteine 315 and cysteine 376 L
A redox-regulated disulphide may form within Tubulin alpha-1A 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 ?
39
PDB code
1ffx
Structure name
tubulin:stathmin-like domain complex
Structure deposition date
2000-07-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
100
Peptide accession
P02550
Residue number A
315
Residue number B
316
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 315 of Tubulin alpha-1A 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-1A 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-1A 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 ?
39
PDB code
7x4n
Structure name
crystal structure of c
Structure deposition date
2022-03-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
77
Peptide accession
P02550
Residue number A
4
Residue number B
129
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 4 of Tubulin alpha-1A 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-1A chain

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 Tubulin alpha-1A 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 ?
39
PDB code
6mze
Structure name
structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (tog) domain arrays
Structure deposition date
2018-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
56
Peptide accession
P02550
Residue number A
316
Residue number B
347
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 316 of Tubulin alpha-1A 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-1A chain

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.

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-1A 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 ?
38
PDB code
6mzf
Structure name
structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (tog) domain arrays
Structure deposition date
2018-11-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
P02550
Residue number A
295
Residue number B
376
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 295 of Tubulin alpha-1A 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-1A chain

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.

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-1A 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 ?
35
PDB code
6mzg
Structure name
structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (tog) domain arrays
Structure deposition date
2018-11-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
P02550
Residue number A
295
Residue number B
315
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 295 of Tubulin alpha-1A 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-1A 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-1A 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
5jco
Structure name
structure and dynamics of single-isoform recombinant neuronal human tubulin
Structure deposition date
2016-04-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q71U36
Residue number A
315
Residue number B
347
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 315 of Tubulin alpha-1A 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-1A chain

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.

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-1A 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 ?
32
PDB code
1ffx
Structure name
tubulin:stathmin-like domain complex
Structure deposition date
2000-07-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
96
Peptide accession
P02550
Residue number A
316
Residue number B
376
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 316 of Tubulin alpha-1A 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-1A chain

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.

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-1A 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 ?
32
PDB code
3j6p
Structure name
pseudo-atomic model of dynein microtubule binding domain-tubulin complex based on a cryoem map
Structure deposition date
2014-03-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
80
Peptide accession
P02550
Residue number A
20
Residue number B
25
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 20 of Tubulin alpha-1A chain

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.

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 25 of Tubulin alpha-1A chain

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.

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-1A 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
6mzg
Structure name
structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (tog) domain arrays
Structure deposition date
2018-11-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
P02550
Residue number A
200
Residue number B
316
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 200 of Tubulin alpha-1A chain

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.

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-1A 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-1A chain between cysteines 4 and 20. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5jco
Structure name
structure and dynamics of single-isoform recombinant neuronal human tubulin
Structure deposition date
2016-04-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
Q71U36
Residue number A
4
Residue number B
20
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 4 of Tubulin alpha-1A 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 20 of Tubulin alpha-1A chain

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.

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-1A chain between cysteines 315 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
3j6f
Structure name
minimized average structure of gdp-bound dynamic microtubules
Structure deposition date
2014-02-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
P02550
Residue number A
315
Residue number B
376
Peptide name
Tubulin alpha-1A chain

Ligandability

Cysteine 315 of Tubulin alpha-1A 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-1A chain

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.

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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