ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Cyclin-dependent kinase 5 activator 1

Intermolecular
Cysteine 261 and cysteine 261
Cysteine 53 of Cyclin-dependent kinase 5 and cysteine 261
Intramolecular
Cysteine 208 and cysteine 229
Cysteine 160 and cysteine 163
Cysteine 229 and cysteine 261
Cysteine 163 and cysteine 208
Cysteine 163 and cysteine 189
Cysteine 208 and cysteine 92
A redox-regulated disulphide may form between two units of Cyclin-dependent kinase 5 activator 1 at cysteines 261 and 261 (357 and 357 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6ldp
Structure name
structure of cdk5r1-bound fem1c
Structure deposition date
2019-11-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
92
Peptide A name
Cyclin-dependent kinase 5 activator 1
Peptide B name
Cyclin-dependent kinase 5 activator 1
Peptide A accession
Q15078
Peptide B accession
Q15078
Peptide A residue number
261
Peptide B residue number
261

Ligandability

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 between cysteine 53 of Cyclin-dependent kinase 5 and cysteine 261 of Cyclin-dependent kinase 5 activator 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
7vdq
Structure name
the structure of cyclin-dependent kinase 5 (cdk5) in complex with p25 and compound 7
Structure deposition date
2021-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
100
Peptide A name
Cyclin-dependent kinase 5
Peptide B name
Cyclin-dependent kinase 5 activator 1
Peptide A accession
Q00535
Peptide B accession
Q15078
Peptide A residue number
53
Peptide B residue number
261

Ligandability

Cysteine 53 of Cyclin-dependent kinase 5

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 261 of Cyclin-dependent kinase 5 activator 1

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 Cyclin-dependent kinase 5 activator 1 between cysteines 208 and 229.

Details

Redox score ?
68
PDB code
1unh
Structure name
structural mechanism for the inhibition of cdk5-p25 by roscovitine, aloisine and indirubin
Structure deposition date
2003-09-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
100
Peptide accession
Q15078
Residue number A
208
Residue number B
229
Peptide name
Cyclin-dependent kinase 5 activator 1

Ligandability

Cysteine 208 of Cyclin-dependent kinase 5 activator 1

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 229 of Cyclin-dependent kinase 5 activator 1

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 Cyclin-dependent kinase 5 activator 1 between cysteines 160 and 163. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1ung
Structure name
structural mechanism for the inhibition of cdk5-p25 by roscovitine, aloisine and indirubin
Structure deposition date
2003-09-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
30
Minimum pKa ?
9
% buried
0
Peptide accession
Q15078
Residue number A
160
Residue number B
163
Peptide name
Cyclin-dependent kinase 5 activator 1

Ligandability

Cysteine 160 of Cyclin-dependent kinase 5 activator 1

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 Cyclin-dependent kinase 5 activator 1

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 Cyclin-dependent kinase 5 activator 1 between cysteines 229 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1unl
Structure name
structural mechanism for the inhibition of cd5-p25 from the roscovitine, aloisine and indirubin
Structure deposition date
2003-09-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
100
Peptide accession
Q15078
Residue number A
229
Residue number B
261
Peptide name
Cyclin-dependent kinase 5 activator 1

Ligandability

Cysteine 229 of Cyclin-dependent kinase 5 activator 1

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 261 of Cyclin-dependent kinase 5 activator 1

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 Cyclin-dependent kinase 5 activator 1 between cysteines 163 and 208. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7vdr
Structure name
the structure of cyclin-dependent kinase 5 (cdk5) in complex with p25 and compound 13
Structure deposition date
2021-09-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
74
Peptide accession
Q15078
Residue number A
163
Residue number B
208
Peptide name
Cyclin-dependent kinase 5 activator 1

Ligandability

Cysteine 163 of Cyclin-dependent kinase 5 activator 1

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 208 of Cyclin-dependent kinase 5 activator 1

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 Cyclin-dependent kinase 5 activator 1 between cysteines 163 and 189 (157 and 189 respectively in this structure).

Details

Redox score ?
nan
PDB code
6ldp
Structure name
structure of cdk5r1-bound fem1c
Structure deposition date
2019-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
96
Peptide accession
Q15078
Residue number A
163
Residue number B
189
Peptide name
Cyclin-dependent kinase 5 activator 1

Ligandability

Cysteine 163 of Cyclin-dependent kinase 5 activator 1

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 189 of Cyclin-dependent kinase 5 activator 1

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 189 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Cyclin-dependent kinase 5 activator 1 between cysteines 208 and 92 (124 and 152 respectively in this structure).

Details

Redox score ?
nan
PDB code
6ldp
Structure name
structure of cdk5r1-bound fem1c
Structure deposition date
2019-11-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
97
Minimum pKa ?
8
% buried
100
Peptide accession
Q15078
Residue number A
208
Residue number B
92
Peptide name
Cyclin-dependent kinase 5 activator 1

Ligandability

Cysteine 208 of Cyclin-dependent kinase 5 activator 1

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 92 of Cyclin-dependent kinase 5 activator 1

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 124 has been assigned to correct residue.
If this tool was useful for finding a disulphide, please cite: