ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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D-ribitol-5-phosphate cytidylyltransferase

Intramolecular
Cysteine 286 and cysteine 335
Cysteine 248 and cysteine 249
Cysteine 229 and cysteine 240
Cysteine 286 and cysteine 340
A redox-regulated disulphide may form within D-ribitol-5-phosphate cytidylyltransferase between cysteines 286 and 335. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
4cvh
Structure name
crystal structure of human isoprenoid synthase domain-containing protein
Structure deposition date
2014-03-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
60
Peptide accession
A4D126
Residue number A
286
Residue number B
335
Peptide name
D-ribitol-5-phosphate cytidylyltransferase

Ligandability

Cysteine 286 of D-ribitol-5-phosphate cytidylyltransferase

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 335 of D-ribitol-5-phosphate cytidylyltransferase

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 D-ribitol-5-phosphate cytidylyltransferase between cysteines 248 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4cvh
Structure name
crystal structure of human isoprenoid synthase domain-containing protein
Structure deposition date
2014-03-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
12
Peptide accession
A4D126
Residue number A
248
Residue number B
249
Peptide name
D-ribitol-5-phosphate cytidylyltransferase

Ligandability

Cysteine 248 of D-ribitol-5-phosphate cytidylyltransferase

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 249 of D-ribitol-5-phosphate cytidylyltransferase

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 D-ribitol-5-phosphate cytidylyltransferase between cysteines 229 and 240. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4cvh
Structure name
crystal structure of human isoprenoid synthase domain-containing protein
Structure deposition date
2014-03-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
64
Peptide accession
A4D126
Residue number A
229
Residue number B
240
Peptide name
D-ribitol-5-phosphate cytidylyltransferase

Ligandability

Cysteine 229 of D-ribitol-5-phosphate cytidylyltransferase

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 240 of D-ribitol-5-phosphate cytidylyltransferase

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 D-ribitol-5-phosphate cytidylyltransferase between cysteines 286 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
4cvh
Structure name
crystal structure of human isoprenoid synthase domain-containing protein
Structure deposition date
2014-03-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
76
Peptide accession
A4D126
Residue number A
286
Residue number B
340
Peptide name
D-ribitol-5-phosphate cytidylyltransferase

Ligandability

Cysteine 286 of D-ribitol-5-phosphate cytidylyltransferase

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 340 of D-ribitol-5-phosphate cytidylyltransferase

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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