ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-tubulin complex component 3

Intramolecular
Cysteine 17 and cysteine 18
Cysteine 704 and cysteine 844
Cysteine 325 and cysteine 388 L
A redox-regulated disulphide may form within Gamma-tubulin complex component 3 between cysteines 17 and 18. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7qj1
Structure name
structure of the recombinant human gamma-tubulin ring complex 6-spoked assembly intermediate (spokes 7-12, homogeneous dataset)
Structure deposition date
2021-12-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
24
Peptide accession
Q96CW5
Residue number A
17
Residue number B
18
Peptide name
Gamma-tubulin complex component 3

Ligandability

Cysteine 17 of Gamma-tubulin complex component 3

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 18 of Gamma-tubulin complex component 3

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 3 between cysteines 704 and 844. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
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)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
50
Peptide accession
Q96CW5
Residue number A
704
Residue number B
844
Peptide name
Gamma-tubulin complex component 3

Ligandability

Cysteine 704 of Gamma-tubulin complex component 3

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 844 of Gamma-tubulin complex component 3

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 3 between cysteines 325 and 388. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7qj2
Structure name
structure of recombinant human gamma-tubulin ring complex 8-spoked assembly intermediate (spokes 5-12)
Structure deposition date
2021-12-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
80
Peptide accession
Q96CW5
Residue number A
325
Residue number B
388
Peptide name
Gamma-tubulin complex component 3

Ligandability

Cysteine 325 of Gamma-tubulin complex component 3

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 388 of Gamma-tubulin complex component 3

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.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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