ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Thymidylate synthase

Intermolecular
Cysteine 174 and cysteine 174
Intramolecular
Cysteine 193 and cysteine 204
Cysteine 174 and cysteine 193
A redox-regulated disulphide may form between two units of Thymidylate synthase at cysteines 174 and 174.

Details

Redox score ?
63
PDB code
5fct
Structure name
mouse thymidylate synthase in ternary complex with fdump and methylenetetrahydrofolate
Structure deposition date
2015-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
93
Minimum pKa ?
9
% buried
100
Peptide A name
Thymidylate synthase
Peptide B name
Thymidylate synthase
Peptide A accession
Q544L2
Peptide B accession
Q544L2
Peptide A residue number
174
Peptide B residue number
174

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 193 and 204.

Details

Redox score ?
61
PDB code
5fct
Structure name
mouse thymidylate synthase in ternary complex with fdump and methylenetetrahydrofolate
Structure deposition date
2015-12-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
100
Peptide accession
Q544L2
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.

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 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.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Thymidylate synthase between cysteines 174 and 193. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5fct
Structure name
mouse thymidylate synthase in ternary complex with fdump and methylenetetrahydrofolate
Structure deposition date
2015-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
9
% buried
100
Peptide accession
Q544L2
Residue number A
174
Residue number B
193
Peptide name
Thymidylate synthase

Ligandability

Cysteine 174 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 193 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.

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