ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-tubulin complex component 6

Intramolecular
Cysteine 169 and cysteine 171
Cysteine 296 and cysteine 302 L
Cysteine 406 and cysteine 477
A redox-regulated disulphide may form within Gamma-tubulin complex component 6 between cysteines 169 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7qj9
Structure name
structure of recombinant human gamma-tubulin ring complex 10-spoked assembly intermediate (spokes 3-12, homogeneous dataset)
Structure deposition date
2021-12-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
43
Minimum pKa ?
10
% buried
20
Peptide accession
Q96RT7
Residue number A
169
Residue number B
171
Peptide name
Gamma-tubulin complex component 6

Ligandability

Cysteine 169 of Gamma-tubulin complex component 6

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 171 of Gamma-tubulin complex component 6

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 Gamma-tubulin complex component 6 between cysteines 296 and 302. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7qj9
Structure name
structure of recombinant human gamma-tubulin ring complex 10-spoked assembly intermediate (spokes 3-12, homogeneous dataset)
Structure deposition date
2021-12-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
8
% buried
58
Peptide accession
Q96RT7
Residue number A
296
Residue number B
302
Peptide name
Gamma-tubulin complex component 6

Ligandability

Cysteine 296 of Gamma-tubulin complex component 6

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 302 of Gamma-tubulin complex component 6

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.

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 Gamma-tubulin complex component 6 between cysteines 406 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7qj0
Structure name
structure of recombinant human gamma-tubulin ring complex 6-spoked assembly intermediate (spokes 7-12)
Structure deposition date
2021-12-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
73
Peptide accession
Q96RT7
Residue number A
406
Residue number B
477
Peptide name
Gamma-tubulin complex component 6

Ligandability

Cysteine 406 of Gamma-tubulin complex component 6

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 477 of Gamma-tubulin complex component 6

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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