ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cell division cycle protein 16 homolog

Intramolecular
Cysteine 250 and cysteine 267
Cysteine 245 and cysteine 250
Cysteine 133 and cysteine 163
A redox-regulated disulphide may form within Cell division cycle protein 16 homolog between cysteines 250 and 267. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3hym
Structure name
insights into anaphase promoting complex tpr subdomain assembly from a cdc26-apc6 structure
Structure deposition date
2009-06-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
11
% buried
56
Peptide accession
Q13042
Residue number A
250
Residue number B
267
Peptide name
Cell division cycle protein 16 homolog

Ligandability

Cysteine 250 of Cell division cycle protein 16 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 267 of Cell division cycle protein 16 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 cycle protein 16 homolog between cysteines 245 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3hym
Structure name
insights into anaphase promoting complex tpr subdomain assembly from a cdc26-apc6 structure
Structure deposition date
2009-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
78
Peptide accession
Q13042
Residue number A
245
Residue number B
250
Peptide name
Cell division cycle protein 16 homolog

Ligandability

Cysteine 245 of Cell division cycle protein 16 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 250 of Cell division cycle protein 16 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 cycle protein 16 homolog between cysteines 133 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6q6h
Structure name
cryo-em structure of the apc/c-cdc20-cdk2-cyclina2-cks2 complex, the d2 box class
Structure deposition date
2018-12-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
74
Peptide accession
Q13042
Residue number A
133
Residue number B
163
Peptide name
Cell division cycle protein 16 homolog

Ligandability

Cysteine 133 of Cell division cycle protein 16 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 163 of Cell division cycle protein 16 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.

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