ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-tubulin complex component 2

Intramolecular
Cysteine 733 and cysteine 737
Cysteine 648 and cysteine 755
Cysteine 648 and cysteine 737
A redox-regulated disulphide may form within Gamma-tubulin complex component 2 between cysteines 733 and 737 (761 and 765 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
6v6b
Structure name
structures of gcp2 and gcp3 in the native human gamma-tubulin ring complex
Structure deposition date
2019-12-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
12
% buried
80
Peptide accession
Q9BSJ2
Residue number A
733
Residue number B
737
Peptide name
Gamma-tubulin complex component 2

Ligandability

Cysteine 733 of Gamma-tubulin complex component 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 737 of Gamma-tubulin complex component 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.

A redox-regulated disulphide may form within Gamma-tubulin complex component 2 between cysteines 648 and 755. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7qj6
Structure name
structure of recombinant human gamma-tubulin ring complex 10-spoked assembly intermediate (spokes 3-12, substoichiometric spokes 13-14)
Structure deposition date
2021-12-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
98
Peptide accession
Q9BSJ2
Residue number A
648
Residue number B
755
Peptide name
Gamma-tubulin complex component 2

Ligandability

Cysteine 648 of Gamma-tubulin complex component 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 755 of Gamma-tubulin complex component 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.

A redox-regulated disulphide may form within Gamma-tubulin complex component 2 between cysteines 648 and 737. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
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)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
100
Peptide accession
Q9BSJ2
Residue number A
648
Residue number B
737
Peptide name
Gamma-tubulin complex component 2

Ligandability

Cysteine 648 of Gamma-tubulin complex component 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 737 of Gamma-tubulin complex component 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.

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