ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Farnesyl pyrophosphate synthase

Intramolecular
Cysteine 157 and cysteine 213
Cysteine 157 and cysteine 204 L
A redox-regulated disulphide may form within Farnesyl pyrophosphate synthase between cysteines 157 and 213 (91 and 147 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5cg5
Structure name
neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate
Structure deposition date
2015-07-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14324
Residue number A
157
Residue number B
213
Peptide name
Farnesyl pyrophosphate synthase

Ligandability

Cysteine 157 of Farnesyl pyrophosphate 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 213 of Farnesyl pyrophosphate 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 Farnesyl pyrophosphate synthase between cysteines 157 and 204 (91 and 138 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5cg6
Structure name
neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate and isopentenyl pyrophosphate
Structure deposition date
2015-07-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14324
Residue number A
157
Residue number B
204
Peptide name
Farnesyl pyrophosphate synthase

Ligandability

Cysteine 157 of Farnesyl pyrophosphate 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 Farnesyl pyrophosphate 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.

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