ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cystathionine gamma-lyase

Intramolecular
Cysteine 137 and cysteine 172
Cysteine 307 and cysteine 310
Cysteine 252 and cysteine 255 L
Cysteine 109 and cysteine 137
Cysteine 84 and cysteine 255 L
Cysteine 84 and cysteine 252 L
Cysteine 70 and cysteine 252 L
A redox-regulated disulphide may form within Cystathionine gamma-lyase between cysteines 137 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3cog
Structure name
crystal structure of human cystathionase (cystathionine gamma lyase) in complex with dl-propargylglycine
Structure deposition date
2008-03-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
86
Peptide accession
P32929
Residue number A
137
Residue number B
172
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 137 of Cystathionine gamma-lyase

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 172 of Cystathionine gamma-lyase

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 Cystathionine gamma-lyase between cysteines 307 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6ovg
Structure name
l-methionine depletion with an engineered human enzyme disrupts prostate cancer metabolism
Structure deposition date
2019-05-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
P32929
Residue number A
307
Residue number B
310
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 307 of Cystathionine gamma-lyase

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 310 of Cystathionine gamma-lyase

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 Cystathionine gamma-lyase between cysteines 252 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6ovg
Structure name
l-methionine depletion with an engineered human enzyme disrupts prostate cancer metabolism
Structure deposition date
2019-05-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
P32929
Residue number A
252
Residue number B
255
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 252 of Cystathionine gamma-lyase

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.

Cysteine 255 of Cystathionine gamma-lyase

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.

A redox-regulated disulphide may form within Cystathionine gamma-lyase between cysteines 109 and 137 (128 and 156 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
5tt2
Structure name
inactive conformation of engineered human cystathionine gamma lyase (e59n, r119l, e339v) to depleting methionine
Structure deposition date
2016-10-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
89
Peptide accession
P32929
Residue number A
109
Residue number B
137
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 109 of Cystathionine gamma-lyase

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 137 of Cystathionine gamma-lyase

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 Cystathionine gamma-lyase between cysteines 84 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3elp
Structure name
structure of cystationine gamma lyase
Structure deposition date
2008-09-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
P32929
Residue number A
84
Residue number B
255
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 84 of Cystathionine gamma-lyase

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 255 of Cystathionine gamma-lyase

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.

A redox-regulated disulphide may form within Cystathionine gamma-lyase between cysteines 84 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
5tsu
Structure name
active conformation for engineered human cystathionine gamma lyase (e59n, r119l, e339v) to depleting methionine
Structure deposition date
2016-10-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
P32929
Residue number A
84
Residue number B
252
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 84 of Cystathionine gamma-lyase

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 252 of Cystathionine gamma-lyase

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.

A redox-regulated disulphide may form within Cystathionine gamma-lyase between cysteines 70 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
6ovg
Structure name
l-methionine depletion with an engineered human enzyme disrupts prostate cancer metabolism
Structure deposition date
2019-05-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
98
Peptide accession
P32929
Residue number A
70
Residue number B
252
Peptide name
Cystathionine gamma-lyase

Ligandability

Cysteine 70 of Cystathionine gamma-lyase

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 252 of Cystathionine gamma-lyase

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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