ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tubulin alpha-1B chain

Intermolecular
Cysteine 158 of Tubulinyl-Tyr carboxypeptidase 2 and cysteine 450
Intramolecular
Cysteine 315 and cysteine 316 L
Cysteine 4 and cysteine 129
Cysteine 295 and cysteine 376 L
Cysteine 295 and cysteine 315 L
Cysteine 315 and cysteine 347 L
Cysteine 295 and cysteine 316 L
Cysteine 316 and cysteine 376 L
Cysteine 20 and cysteine 25
Cysteine 200 and cysteine 316 L
More...
Cysteine 316 and cysteine 347 L
Cysteine 4 and cysteine 20
Cysteine 315 and cysteine 376 L
A redox-regulated disulphide may form between cysteine 158 of Tubulinyl-Tyr carboxypeptidase 2 and cysteine 450 of Tubulin alpha-1B chain.

Details

Redox score ?
83
PDB code
6j4v
Structure name
structural basis of tubulin detyrosination by vasohibins-svbp enzyme complex and functional implications
Structure deposition date
2019-01-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Tubulinyl-Tyr carboxypeptidase 2
Peptide B name
Tubulin alpha-1B chain
Peptide A accession
Q86V25
Peptide B accession
P68363
Peptide A residue number
158
Peptide B residue number
450

Ligandability

Cysteine 158 of Tubulinyl-Tyr carboxypeptidase 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 450 of Tubulin alpha-1B 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 450 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Tubulin alpha-1B 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 ?
40
PDB code
7pjf
Structure name
inhibiting parasite proliferation using a rationally designed anti- tubulin agent
Structure deposition date
2021-08-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
92
Peptide accession
P68363
Residue number A
315
Residue number B
316
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 315 of Tubulin alpha-1B 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 316 of Tubulin alpha-1B 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-1B 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
4i50
Structure name
crystal structure of tubulin-stathmin-ttl-epothilone a complex
Structure deposition date
2012-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
80
Peptide accession
P81947
Residue number A
4
Residue number B
129
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 4 of Tubulin alpha-1B 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-1B 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-1B 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
6x1f
Structure name
tubulin-rb3_sld-ttl in complex with compound 5m
Structure deposition date
2020-05-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q2XVP4
Residue number A
295
Residue number B
376
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 295 of Tubulin alpha-1B 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-1B 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-1B 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 ?
37
PDB code
6s8l
Structure name
structure, thermodynamics, and kinetics of plinabulin binding to two tubulin isotypes
Structure deposition date
2019-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
P68363
Residue number A
295
Residue number B
315
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 295 of Tubulin alpha-1B 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 315 of Tubulin alpha-1B 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.

A redox-regulated disulphide may form within Tubulin alpha-1B 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 ?
32
PDB code
6xer
Structure name
tubulin-rb3_sld in complex with colchicine
Structure deposition date
2020-06-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
Q2XVP4
Residue number A
315
Residue number B
347
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 315 of Tubulin alpha-1B 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 347 of Tubulin alpha-1B chain

Not ligandable in the dataset of Yang et al.

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-1B chain between cysteines 295 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6ta3
Structure name
human kinesin-5 motor domain in the gsk-1 state bound to microtubules (conformation 1)
Structure deposition date
2019-10-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
Q2XVP4
Residue number A
295
Residue number B
316
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 295 of Tubulin alpha-1B 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 316 of Tubulin alpha-1B 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-1B 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
5s5u
Structure name
tubulin-z1124201124-complex
Structure deposition date
2020-11-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
P81947
Residue number A
316
Residue number B
376
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 316 of Tubulin alpha-1B 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.

Cysteine 376 of Tubulin alpha-1B 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-1B 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
5ij0
Structure name
cryo em density of microtubule assembled from human tubb3
Structure deposition date
2016-03-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
92
Peptide accession
P68363
Residue number A
20
Residue number B
25
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 20 of Tubulin alpha-1B 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 25 of Tubulin alpha-1B 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-1B 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 ?
30
PDB code
7pjf
Structure name
inhibiting parasite proliferation using a rationally designed anti- tubulin agent
Structure deposition date
2021-08-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
92
Peptide accession
P68363
Residue number A
200
Residue number B
316
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 200 of Tubulin alpha-1B 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-1B 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-1B 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 ?
29
PDB code
6i2i
Structure name
refined 13pf hela cell tubulin microtubule (eml4-ntd decorated)
Structure deposition date
2018-11-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
P68363
Residue number A
316
Residue number B
347
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 316 of Tubulin alpha-1B 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.

Cysteine 347 of Tubulin alpha-1B chain

Not ligandable in the dataset of Yang et al.

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-1B 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
7pqp
Structure name
tau-microtubule structural ensemble based on cryoem data
Structure deposition date
2021-09-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q2XVP4
Residue number A
4
Residue number B
20
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 4 of Tubulin alpha-1B 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-1B 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-1B 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 ?
20
PDB code
6wwl
Structure name
kif14[391-755] dimer two-heads-bound state - amp-pnp in complex with a microtubule
Structure deposition date
2020-05-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
Q2XVP4
Residue number A
315
Residue number B
376
Peptide name
Tubulin alpha-1B chain

Ligandability

Cysteine 315 of Tubulin alpha-1B 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 376 of Tubulin alpha-1B 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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