ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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L-serine dehydratase/L-threonine deaminase

Intramolecular
Cysteine 306 and cysteine 339
Cysteine 49 and cysteine 57
Cysteine 49 and cysteine 62
A redox-regulated disulphide may form within L-serine dehydratase/L-threonine deaminase between cysteines 306 and 339 (270 and 303 respectively in this structure).

Details

Redox score ?
65
PDB code
1pwe
Structure name
rat liver l-serine dehydratase apo enzyme
Structure deposition date
2003-07-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
8
% buried
100
Peptide accession
P09367
Residue number A
306
Residue number B
339
Peptide name
L-serine dehydratase/L-threonine deaminase

Ligandability

Cysteine 306 of L-serine dehydratase/L-threonine deaminase

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 L-serine dehydratase/L-threonine deaminase

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 L-serine dehydratase/L-threonine deaminase between cysteines 49 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4h27
Structure name
modulating the function of human serine racemase and human serine dehydratase by protein engineering
Structure deposition date
2012-09-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
69
Peptide accession
P20132
Residue number A
49
Residue number B
57
Peptide name
L-serine dehydratase/L-threonine deaminase

Ligandability

Cysteine 49 of L-serine dehydratase/L-threonine deaminase

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 57 of L-serine dehydratase/L-threonine deaminase

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 L-serine dehydratase/L-threonine deaminase between cysteines 49 and 62. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1p5j
Structure name
crystal structure analysis of human serine dehydratase
Structure deposition date
2003-04-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
100
Peptide accession
P20132
Residue number A
49
Residue number B
62
Peptide name
L-serine dehydratase/L-threonine deaminase

Ligandability

Cysteine 49 of L-serine dehydratase/L-threonine deaminase

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 62 of L-serine dehydratase/L-threonine deaminase

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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