ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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G1/S-specific cyclin-E1

Intramolecular
Cysteine 285 and cysteine 327
Cysteine 285 and cysteine 291
Cysteine 291 and cysteine 327
A redox-regulated disulphide may form within G1/S-specific cyclin-E1 between cysteines 285 and 327 (270 and 312 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5l2w
Structure name
the x-ray co-crystal structure of human cdk2/cycline and dinaciclib
Structure deposition date
2016-08-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
92
Peptide accession
P24864
Residue number A
285
Residue number B
327
Peptide name
G1/S-specific cyclin-E1

Ligandability

Cysteine 285 of G1/S-specific cyclin-E1

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 327 of G1/S-specific cyclin-E1

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 G1/S-specific cyclin-E1 between cysteines 285 and 291 (270 and 276 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7kjs
Structure name
crystal structure of cdk2/cyclin e in complex with pf-06873600
Structure deposition date
2020-10-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
P24864
Residue number A
285
Residue number B
291
Peptide name
G1/S-specific cyclin-E1

Ligandability

Cysteine 285 of G1/S-specific cyclin-E1

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 291 of G1/S-specific cyclin-E1

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 G1/S-specific cyclin-E1 between cysteines 291 and 327 (276 and 312 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
1w98
Structure name
the structural basis of cdk2 activation by cyclin e
Structure deposition date
2004-10-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
93
Peptide accession
P24864
Residue number A
291
Residue number B
327
Peptide name
G1/S-specific cyclin-E1

Ligandability

Cysteine 291 of G1/S-specific cyclin-E1

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 327 of G1/S-specific cyclin-E1

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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