ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cell division control protein 6 homolog

Intramolecular
Cysteine 191 and cysteine 466
Cysteine 394 and cysteine 233
Cysteine 211 and cysteine 65
Cysteine 146 and cysteine 211
A redox-regulated disulphide may form within Cell division control protein 6 homolog between cysteines 191 and 466 (172 and 174 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
4i5l
Structure name
structural mechanism of trimeric pp2a holoenzyme involving pr70: insight for cdc6 dephosphorylation
Structure deposition date
2012-11-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
88
Peptide accession
Q99741
Residue number A
191
Residue number B
466
Peptide name
Cell division control protein 6 homolog

Ligandability

Cysteine 191 of Cell division control protein 6 homolog

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 466 of Cell division control protein 6 homolog

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.

Uncertain whether structure cysteine 174 has been assigned to correct residue.
A redox-regulated disulphide may form within Cell division control protein 6 homolog between cysteines 394 and 233 (210 and 283 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
4i5n
Structure name
structural mechanism of trimeric pp2a holoenzyme involving pr70: insight for cdc6 dephosphorylation
Structure deposition date
2012-11-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
60
Peptide accession
Q99741
Residue number A
394
Residue number B
233
Peptide name
Cell division control protein 6 homolog

Ligandability

Cysteine 394 of Cell division control protein 6 homolog

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 233 of Cell division control protein 6 homolog

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 Cell division control protein 6 homolog between cysteines 211 and 65 (437 and 439 respectively in this structure).

Details

Redox score ?
nan
PDB code
4i5l
Structure name
structural mechanism of trimeric pp2a holoenzyme involving pr70: insight for cdc6 dephosphorylation
Structure deposition date
2012-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
76
Peptide accession
Q99741
Residue number A
211
Residue number B
65
Peptide name
Cell division control protein 6 homolog

Ligandability

Cysteine 211 of Cell division control protein 6 homolog

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 65 of Cell division control protein 6 homolog

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.

Uncertain whether structure cysteine 437 has been assigned to correct residue.
A redox-regulated disulphide may form within Cell division control protein 6 homolog between cysteines 146 and 211 (421 and 437 respectively in this structure).

Details

Redox score ?
nan
PDB code
4i5l
Structure name
structural mechanism of trimeric pp2a holoenzyme involving pr70: insight for cdc6 dephosphorylation
Structure deposition date
2012-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
62
Peptide accession
Q99741
Residue number A
146
Residue number B
211
Peptide name
Cell division control protein 6 homolog

Ligandability

Cysteine 146 of Cell division control protein 6 homolog

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 211 of Cell division control protein 6 homolog

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.

Uncertain whether structure cysteine 421 has been assigned to correct residue.
Uncertain whether structure cysteine 437 has been assigned to correct residue.
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