ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cyclin-dependent kinase 13

Intramolecular
Cysteine 987 and cysteine 995 L
Cysteine 902 and cysteine 930 L
Cysteine 840 and cysteine 902 L
Cysteine 900 and cysteine 987 L
Cysteine 900 and cysteine 902
Cysteine 828 and cysteine 900
Cysteine 840 and cysteine 900 L
A redox-regulated disulphide may form within Cyclin-dependent kinase 13 between cysteines 987 and 995. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
5efq
Structure name
crystal structure of human cdk13/cyclin k in complex with adp-aluminum fluoride
Structure deposition date
2015-10-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
66
Peptide accession
Q14004
Residue number A
987
Residue number B
995
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 987 of Cyclin-dependent kinase 13

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 995 of Cyclin-dependent kinase 13

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cyclin-dependent kinase 13 between cysteines 902 and 930. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5efq
Structure name
crystal structure of human cdk13/cyclin k in complex with adp-aluminum fluoride
Structure deposition date
2015-10-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
100
Peptide accession
Q14004
Residue number A
902
Residue number B
930
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 902 of Cyclin-dependent kinase 13

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 930 of Cyclin-dependent kinase 13

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cyclin-dependent kinase 13 between cysteines 840 and 902. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
7nxj
Structure name
crystal structure of human cdk13/cyclin k in complex with the inhibitor thz531
Structure deposition date
2021-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
98
Peptide accession
Q14004
Residue number A
840
Residue number B
902
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 840 of Cyclin-dependent kinase 13

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.

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 902 of Cyclin-dependent kinase 13

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 13 between cysteines 900 and 987. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5efq
Structure name
crystal structure of human cdk13/cyclin k in complex with adp-aluminum fluoride
Structure deposition date
2015-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
91
Peptide accession
Q14004
Residue number A
900
Residue number B
987
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 900 of Cyclin-dependent kinase 13

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 987 of Cyclin-dependent kinase 13

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Cyclin-dependent kinase 13 between cysteines 900 and 902. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
7nxj
Structure name
crystal structure of human cdk13/cyclin k in complex with the inhibitor thz531
Structure deposition date
2021-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q14004
Residue number A
900
Residue number B
902
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 900 of Cyclin-dependent kinase 13

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 902 of Cyclin-dependent kinase 13

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 13 between cysteines 828 and 900. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
5efq
Structure name
crystal structure of human cdk13/cyclin k in complex with adp-aluminum fluoride
Structure deposition date
2015-10-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q14004
Residue number A
828
Residue number B
900
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 828 of Cyclin-dependent kinase 13

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 900 of Cyclin-dependent kinase 13

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 13 between cysteines 840 and 900. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
20
PDB code
5efq
Structure name
crystal structure of human cdk13/cyclin k in complex with adp-aluminum fluoride
Structure deposition date
2015-10-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
14
% buried
100
Peptide accession
Q14004
Residue number A
840
Residue number B
900
Peptide name
Cyclin-dependent kinase 13

Ligandability

Cysteine 840 of Cyclin-dependent kinase 13

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.

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 900 of Cyclin-dependent kinase 13

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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