ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tubulin beta chain

Intramolecular
Cysteine 220 and cysteine 335
Cysteine 108 and cysteine 110
Cysteine 182 and cysteine 284
A redox-regulated disulphide may form within Tubulin beta chain between cysteines 220 and 335 (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 ?
55
PDB code
5jcb
Structure name
microtubule depolymerizing agent podophyllotoxin derivative yjtsf1
Structure deposition date
2016-04-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
86
Peptide accession
F2Z5B2
Residue number A
220
Residue number B
335
Peptide name
Tubulin beta chain

Ligandability

Cysteine 220 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 335 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 108 and 110 (127 and 129 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5ca0
Structure name
crystal structure of t2r-ttl-lexibulin complex
Structure deposition date
2015-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
11
% buried
61
Peptide accession
F2Z5B2
Residue number A
108
Residue number B
110
Peptide name
Tubulin beta chain

Ligandability

Cysteine 108 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 110 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 182 and 284 (201 and 303 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5xp3
Structure name
crystal structure of apo t2r-ttl
Structure deposition date
2017-05-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
F2Z5B2
Residue number A
182
Residue number B
284
Peptide name
Tubulin beta chain

Ligandability

Cysteine 182 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 284 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.

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