ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-acylneuraminate cytidylyltransferase

Intramolecular
Cysteine 278 and cysteine 283
Cysteine 403 and cysteine 405
Cysteine 283 and cysteine 403
Cysteine 278 and cysteine 339
Cysteine 278 and cysteine 403
A redox-regulated disulphide may form within N-acylneuraminate cytidylyltransferase between cysteines 278 and 283 (14 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
3ewi
Structure name
structural analysis of the c-terminal domain of murine cmp-sialic acid synthetase
Structure deposition date
2008-10-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
100
Peptide accession
Q99KK2
Residue number A
278
Residue number B
283
Peptide name
N-acylneuraminate cytidylyltransferase

Ligandability

Cysteine 278 of N-acylneuraminate 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 283 of N-acylneuraminate 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 N-acylneuraminate cytidylyltransferase between cysteines 403 and 405 (139 and 141 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3ewi
Structure name
structural analysis of the c-terminal domain of murine cmp-sialic acid synthetase
Structure deposition date
2008-10-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
39
Peptide accession
Q99KK2
Residue number A
403
Residue number B
405
Peptide name
N-acylneuraminate cytidylyltransferase

Ligandability

Cysteine 403 of N-acylneuraminate 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 405 of N-acylneuraminate 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 N-acylneuraminate cytidylyltransferase between cysteines 283 and 403 (19 and 139 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3ewi
Structure name
structural analysis of the c-terminal domain of murine cmp-sialic acid synthetase
Structure deposition date
2008-10-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
84
Peptide accession
Q99KK2
Residue number A
283
Residue number B
403
Peptide name
N-acylneuraminate cytidylyltransferase

Ligandability

Cysteine 283 of N-acylneuraminate 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 403 of N-acylneuraminate 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 N-acylneuraminate cytidylyltransferase between cysteines 278 and 339 (14 and 75 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3ewi
Structure name
structural analysis of the c-terminal domain of murine cmp-sialic acid synthetase
Structure deposition date
2008-10-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
82
Peptide accession
Q99KK2
Residue number A
278
Residue number B
339
Peptide name
N-acylneuraminate cytidylyltransferase

Ligandability

Cysteine 278 of N-acylneuraminate 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 339 of N-acylneuraminate 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 N-acylneuraminate cytidylyltransferase between cysteines 278 and 403 (14 and 139 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3ewi
Structure name
structural analysis of the c-terminal domain of murine cmp-sialic acid synthetase
Structure deposition date
2008-10-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
84
Peptide accession
Q99KK2
Residue number A
278
Residue number B
403
Peptide name
N-acylneuraminate cytidylyltransferase

Ligandability

Cysteine 278 of N-acylneuraminate 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 403 of N-acylneuraminate 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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