ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Tubulin beta chain

Intramolecular
Cysteine 127 and cysteine 129
Cysteine 239 and cysteine 354
Cysteine 203 and cysteine 303
A redox-regulated disulphide may form within Tubulin beta chain between cysteines 127 and 129 (129 and 131 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4hna
Structure name
kinesin motor domain in the adp-mg-alfx state in complex with tubulin and a darpin
Structure deposition date
2012-10-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
11
% buried
60
Peptide accession
D0VWY9
Residue number A
127
Residue number B
129
Peptide name
Tubulin beta chain

Ligandability

Cysteine 127 of Tubulin beta 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 beta 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 beta chain between cysteines 239 and 354 (241 and 356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5kx5
Structure name
crystal structure of tubulin-stathmin-ttl-compound 11 complex
Structure deposition date
2016-07-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
88
Peptide accession
D0VWY9
Residue number A
239
Residue number B
354
Peptide name
Tubulin beta chain

Ligandability

Cysteine 239 of Tubulin beta 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 354 of Tubulin beta 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 beta chain between cysteines 203 and 303 (203 and 305 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
6gvm
Structure name
tubulin:f3ii darpin complex
Structure deposition date
2018-06-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
D0VWY9
Residue number A
203
Residue number B
303
Peptide name
Tubulin beta chain

Ligandability

Cysteine 203 of Tubulin beta 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 303 of Tubulin beta 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 203 in protein A could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: