ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-tubulin complex component 4

Intramolecular
Cysteine 495 and cysteine 594
Cysteine 590 and cysteine 594
Cysteine 495 and cysteine 590
Cysteine 90 and cysteine 179
Cysteine 151 and cysteine 179
A redox-regulated disulphide may form within Gamma-tubulin complex component 4 between cysteines 495 and 594 (494 and 593 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3rip
Structure name
crystal structure of human gamma-tubulin complex protein 4 (gcp4)
Structure deposition date
2011-04-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UGJ1
Residue number A
495
Residue number B
594
Peptide name
Gamma-tubulin complex component 4

Ligandability

Cysteine 495 of Gamma-tubulin complex component 4

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 594 of Gamma-tubulin complex component 4

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 4 between cysteines 590 and 594 (589 and 593 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3rip
Structure name
crystal structure of human gamma-tubulin complex protein 4 (gcp4)
Structure deposition date
2011-04-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UGJ1
Residue number A
590
Residue number B
594
Peptide name
Gamma-tubulin complex component 4

Ligandability

Cysteine 590 of Gamma-tubulin complex component 4

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 594 of Gamma-tubulin complex component 4

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 4 between cysteines 495 and 590. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
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 ?
71
Minimum pKa ?
8
% buried
72
Peptide accession
Q9UGJ1
Residue number A
495
Residue number B
590
Peptide name
Gamma-tubulin complex component 4

Ligandability

Cysteine 495 of Gamma-tubulin complex component 4

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 590 of Gamma-tubulin complex component 4

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 4 between cysteines 90 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3rip
Structure name
crystal structure of human gamma-tubulin complex protein 4 (gcp4)
Structure deposition date
2011-04-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
85
Peptide accession
Q9UGJ1
Residue number A
90
Residue number B
179
Peptide name
Gamma-tubulin complex component 4

Ligandability

Cysteine 90 of Gamma-tubulin complex component 4

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 179 of Gamma-tubulin complex component 4

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 4 between cysteines 151 and 179. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3rip
Structure name
crystal structure of human gamma-tubulin complex protein 4 (gcp4)
Structure deposition date
2011-04-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
Q9UGJ1
Residue number A
151
Residue number B
179
Peptide name
Gamma-tubulin complex component 4

Ligandability

Cysteine 151 of Gamma-tubulin complex component 4

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 179 of Gamma-tubulin complex component 4

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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