ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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N-acylneuraminate-9-phosphatase

Intramolecular
Cysteine 145 and cysteine 147
Cysteine 174 and cysteine 184
Cysteine 173 and cysteine 174
Cysteine 49 and cysteine 96
Cysteine 173 and cysteine 184
Cysteine 184 and cysteine 242
A redox-regulated disulphide may form within N-acylneuraminate-9-phosphatase between cysteines 145 and 147.

Details

Redox score ?
79
PDB code
4knv
Structure name
the crystal structure of apo human hdhd4 from se-mad
Structure deposition date
2013-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
72
Peptide accession
Q8TBE9
Residue number A
145
Residue number B
147
Peptide name
N-acylneuraminate-9-phosphatase

Ligandability

Cysteine 145 of N-acylneuraminate-9-phosphatase

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 147 of N-acylneuraminate-9-phosphatase

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-9-phosphatase between cysteines 174 and 184 (176 and 186 respectively in this structure).

Details

Redox score ?
71
PDB code
4knw
Structure name
the crystal structure of human hdhd4 in complex with magnesium and the phosphate mimetic vanadate
Structure deposition date
2013-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8TBE9
Residue number A
174
Residue number B
184
Peptide name
N-acylneuraminate-9-phosphatase

Ligandability

Cysteine 174 of N-acylneuraminate-9-phosphatase

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 184 of N-acylneuraminate-9-phosphatase

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-9-phosphatase between cysteines 173 and 174 (175 and 176 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4knw
Structure name
the crystal structure of human hdhd4 in complex with magnesium and the phosphate mimetic vanadate
Structure deposition date
2013-05-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8TBE9
Residue number A
173
Residue number B
174
Peptide name
N-acylneuraminate-9-phosphatase

Ligandability

Cysteine 173 of N-acylneuraminate-9-phosphatase

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 174 of N-acylneuraminate-9-phosphatase

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-9-phosphatase between cysteines 49 and 96. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2gfh
Structure name
crystal structure of a n-acetylneuraminic acid phosphatase (nanp) from mus musculus at 1
Structure deposition date
2006-03-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
78
Peptide accession
Q9CPT3
Residue number A
49
Residue number B
96
Peptide name
N-acylneuraminate-9-phosphatase

Ligandability

Cysteine 49 of N-acylneuraminate-9-phosphatase

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 96 of N-acylneuraminate-9-phosphatase

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-9-phosphatase between cysteines 173 and 184 (175 and 186 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4knw
Structure name
the crystal structure of human hdhd4 in complex with magnesium and the phosphate mimetic vanadate
Structure deposition date
2013-05-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8TBE9
Residue number A
173
Residue number B
184
Peptide name
N-acylneuraminate-9-phosphatase

Ligandability

Cysteine 173 of N-acylneuraminate-9-phosphatase

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 184 of N-acylneuraminate-9-phosphatase

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-9-phosphatase between cysteines 184 and 242. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4knv
Structure name
the crystal structure of apo human hdhd4 from se-mad
Structure deposition date
2013-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
70
Peptide accession
Q8TBE9
Residue number A
184
Residue number B
242
Peptide name
N-acylneuraminate-9-phosphatase

Ligandability

Cysteine 184 of N-acylneuraminate-9-phosphatase

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 242 of N-acylneuraminate-9-phosphatase

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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