ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cyclin-dependent kinase 12

Intramolecular
Cysteine 924 and cysteine 952
Cysteine 922 and cysteine 924
Cysteine 850 and cysteine 922
Cysteine 922 and cysteine 1009 L
Cysteine 862 and cysteine 924
Cysteine 862 and cysteine 922
A redox-regulated disulphide may form within Cyclin-dependent kinase 12 between cysteines 924 and 952. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7nxk
Structure name
crystal structure of human cdk12/cyclin k in complex with the inhibitor bsj-01-175
Structure deposition date
2021-03-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
100
Peptide accession
Q9NYV4
Residue number A
924
Residue number B
952
Peptide name
Cyclin-dependent kinase 12

Ligandability

Cysteine 924 of Cyclin-dependent kinase 12

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 952 of Cyclin-dependent kinase 12

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 12 between cysteines 922 and 924. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
4nst
Structure name
crystal structure of human cdk12/cyclin k in complex with adp-aluminum fluoride
Structure deposition date
2013-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
Q9NYV4
Residue number A
922
Residue number B
924
Peptide name
Cyclin-dependent kinase 12

Ligandability

Cysteine 922 of Cyclin-dependent kinase 12

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 924 of Cyclin-dependent kinase 12

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 12 between cysteines 850 and 922. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6ckx
Structure name
structure of cdk12/cyck in complex with a small molecule inhibitor n- (4-(1-methyl-1h-pyrazol-4-yl)phenyl)-n-((1r,4r)-4-(quinazolin-2- ylamino)cyclohexyl)acetamide
Structure deposition date
2018-03-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
96
Peptide accession
Q9NYV4
Residue number A
850
Residue number B
922
Peptide name
Cyclin-dependent kinase 12

Ligandability

Cysteine 850 of Cyclin-dependent kinase 12

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 922 of Cyclin-dependent kinase 12

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 12 between cysteines 922 and 1009. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6b3e
Structure name
crystal structure of human cdk12/cyclink in complex with an inhibitor
Structure deposition date
2017-09-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
94
Peptide accession
Q9NYV4
Residue number A
922
Residue number B
1009
Peptide name
Cyclin-dependent kinase 12

Ligandability

Cysteine 922 of Cyclin-dependent kinase 12

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 1009 of Cyclin-dependent kinase 12

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.

A redox-regulated disulphide may form within Cyclin-dependent kinase 12 between cysteines 862 and 924. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
6td3
Structure name
structure of ddb1 bound to cr8-engaged cdk12-cyclink
Structure deposition date
2019-11-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
100
Peptide accession
Q9NYV4
Residue number A
862
Residue number B
924
Peptide name
Cyclin-dependent kinase 12

Ligandability

Cysteine 862 of Cyclin-dependent kinase 12

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 924 of Cyclin-dependent kinase 12

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 12 between cysteines 862 and 922. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
4cxa
Structure name
crystal structure of the human cdk12-cyclin k complex bound to amppnp
Structure deposition date
2014-04-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q9NYV4
Residue number A
862
Residue number B
922
Peptide name
Cyclin-dependent kinase 12

Ligandability

Cysteine 862 of Cyclin-dependent kinase 12

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 922 of Cyclin-dependent kinase 12

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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