ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Adenylosuccinate lyase

Intramolecular
Cysteine 98 and cysteine 99
Cysteine 266 and cysteine 304
Cysteine 303 and cysteine 304
Cysteine 266 and cysteine 305
Cysteine 172 and cysteine 173
Cysteine 304 and cysteine 305
Cysteine 173 and cysteine 180
Cysteine 266 and cysteine 303
Cysteine 303 and cysteine 305
A redox-regulated disulphide may form within Adenylosuccinate lyase between cysteines 98 and 99.

Details

Redox score ?
75
PDB code
2vd6
Structure name
human adenylosuccinate lyase in complex with its substrate n6-(1,2-dicarboxyethyl)-amp, and its products amp and fumarate
Structure deposition date
2007-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
46
Peptide accession
P30566
Residue number A
98
Residue number B
99
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 98 of Adenylosuccinate 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 99 of Adenylosuccinate 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 Adenylosuccinate lyase between cysteines 266 and 304.

Details

Redox score ?
65
PDB code
4ffx
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
P30566
Residue number A
266
Residue number B
304
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 266 of Adenylosuccinate 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 304 of Adenylosuccinate 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 Adenylosuccinate lyase between cysteines 303 and 304. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4flc
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
94
Peptide accession
P30566
Residue number A
303
Residue number B
304
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 303 of Adenylosuccinate 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 304 of Adenylosuccinate 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 303 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Adenylosuccinate lyase between cysteines 266 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4flc
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
90
Minimum pKa ?
15
% buried
100
Peptide accession
P30566
Residue number A
266
Residue number B
305
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 266 of Adenylosuccinate 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 305 of Adenylosuccinate 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 Adenylosuccinate lyase between cysteines 172 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4ffx
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P30566
Residue number A
172
Residue number B
173
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 172 of Adenylosuccinate 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 173 of Adenylosuccinate 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 Adenylosuccinate lyase between cysteines 304 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4flc
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
10
% buried
100
Peptide accession
P30566
Residue number A
304
Residue number B
305
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 304 of Adenylosuccinate 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 305 of Adenylosuccinate 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 Adenylosuccinate lyase between cysteines 173 and 180. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4ffx
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
98
Peptide accession
P30566
Residue number A
173
Residue number B
180
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 173 of Adenylosuccinate 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 180 of Adenylosuccinate 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 Adenylosuccinate lyase between cysteines 266 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4flc
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
96
Peptide accession
P30566
Residue number A
266
Residue number B
303
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 266 of Adenylosuccinate 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 303 of Adenylosuccinate 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 303 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Adenylosuccinate lyase between cysteines 303 and 305.

Details

Redox score ?
nan
PDB code
4flc
Structure name
structural and biochemical characterization of human adenylosuccinate lyase (adsl) and the r303c adsl deficiency associated mutation
Structure deposition date
2012-06-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
94
Peptide accession
P30566
Residue number A
303
Residue number B
305
Peptide name
Adenylosuccinate lyase

Ligandability

Cysteine 303 of Adenylosuccinate 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 305 of Adenylosuccinate 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 303 in protein A could not be asigned to a Uniprot residue.
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