ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Thymidylate synthase

Intermolecular
Cysteine 180 and cysteine 180
Cysteine 43 and cysteine 43
Intramolecular
Cysteine 180 and cysteine 195 L
Cysteine 193 and cysteine 204 L
Cysteine 180 and cysteine 199 L
A redox-regulated disulphide may form between two units of Thymidylate synthase at cysteines 180 and 180.

Details

Redox score ?
66
PDB code
6r2e
Structure name
crystal structure of the human thymidylate synthase (hts) interface variant q62r
Structure deposition date
2019-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
93
Minimum pKa ?
8
% buried
100
Peptide A name
Thymidylate synthase
Peptide B name
Thymidylate synthase
Peptide A accession
P04818
Peptide B accession
P04818
Peptide A residue number
180
Peptide B residue number
180

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 two units of Thymidylate synthase at cysteines 43 and 43. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1juj
Structure name
human thymidylate synthase bound to dump and ly231514, a pyrrolo(2,3- d)pyrimidine-based antifolate
Structure deposition date
2001-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
28
Peptide A name
Thymidylate synthase
Peptide B name
Thymidylate synthase
Peptide A accession
P04818
Peptide B accession
P04818
Peptide A residue number
43
Peptide B residue number
43

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 within Thymidylate synthase between cysteines 180 and 195.

Details

Redox score ?
69
PDB code
5x4x
Structure name
mutant human thymidylate synthase a191k crystallized in a sulfate- containing condition
Structure deposition date
2017-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
44
Peptide accession
P04818
Residue number A
180
Residue number B
195
Peptide name
Thymidylate synthase

Ligandability

Cysteine 180 of Thymidylate synthase

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 195 of Thymidylate synthase

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 Thymidylate synthase between cysteines 193 and 204.

Details

Redox score ?
62
PDB code
4e5o
Structure name
crystal structure of mouse thymidylate synthase in complex with dump
Structure deposition date
2012-03-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
P07607
Residue number A
193
Residue number B
204
Peptide name
Thymidylate synthase

Ligandability

Cysteine 193 of Thymidylate synthase

Not ligandable in the dataset of Yang et al.

Ligandable in the dataset of Yan et al.

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 204 of Thymidylate synthase

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 Thymidylate synthase between cysteines 180 and 199. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
19
PDB code
1ju6
Structure name
human thymidylate synthase complex with dump and ly231514, a pyrrolo(2,3-d)pyrimidine-based antifolate
Structure deposition date
2001-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
17
% buried
100
Peptide accession
P04818
Residue number A
180
Residue number B
199
Peptide name
Thymidylate synthase

Ligandability

Cysteine 180 of Thymidylate synthase

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 199 of Thymidylate synthase

Not ligandable in the dataset of Yang et al.

Ligandable in the dataset of Yan et al.

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.

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