ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glycogen [starch] synthase, muscle

Intramolecular
Cysteine 137 and cysteine 189
Cysteine 137 and cysteine 251
Cysteine 189 and cysteine 251
Cysteine 500 and cysteine 519
Cysteine 243 and cysteine 251
Cysteine 189 and cysteine 191
Cysteine 191 and cysteine 251
Cysteine 137 and cysteine 243
Cysteine 189 and cysteine 243
A redox-regulated disulphide may form within Glycogen [starch] synthase, muscle between cysteines 137 and 189.

Details

Redox score ?
71
PDB code
7q0b
Structure name
human gys1-gyg1 complex inhibited state
Structure deposition date
2021-10-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
97
Peptide accession
P13807
Residue number A
137
Residue number B
189
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 137 of Glycogen [starch] synthase, muscle

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 189 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 137 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
7q13
Structure name
human gys1-gyg1 complex activated state bound to glucose-6-phosphate, uridine diphosphate, and glucose
Structure deposition date
2021-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
89
Peptide accession
P13807
Residue number A
137
Residue number B
251
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 137 of Glycogen [starch] synthase, muscle

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 251 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 189 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
7q13
Structure name
human gys1-gyg1 complex activated state bound to glucose-6-phosphate, uridine diphosphate, and glucose
Structure deposition date
2021-10-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
100
Peptide accession
P13807
Residue number A
189
Residue number B
251
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 189 of Glycogen [starch] synthase, muscle

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 251 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 500 and 519. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7q0s
Structure name
human gys1-gyg1 complex inhibited-like state bound to glucose-6- phosphate
Structure deposition date
2021-10-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
100
Peptide accession
P13807
Residue number A
500
Residue number B
519
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 500 of Glycogen [starch] synthase, muscle

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 519 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 243 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
8cvz
Structure name
human glycogenin-1 and glycogen synthase-1 complex in the apo ordered state
Structure deposition date
2022-05-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
7
% buried
100
Peptide accession
P13807
Residue number A
243
Residue number B
251
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 243 of Glycogen [starch] synthase, muscle

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 251 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 189 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7q13
Structure name
human gys1-gyg1 complex activated state bound to glucose-6-phosphate, uridine diphosphate, and glucose
Structure deposition date
2021-10-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
P13807
Residue number A
189
Residue number B
191
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 189 of Glycogen [starch] synthase, muscle

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 191 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 191 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
8cvz
Structure name
human glycogenin-1 and glycogen synthase-1 complex in the apo ordered state
Structure deposition date
2022-05-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
99
Peptide accession
P13807
Residue number A
191
Residue number B
251
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 191 of Glycogen [starch] synthase, muscle

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 251 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 137 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
8cvz
Structure name
human glycogenin-1 and glycogen synthase-1 complex in the apo ordered state
Structure deposition date
2022-05-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P13807
Residue number A
137
Residue number B
243
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 137 of Glycogen [starch] synthase, muscle

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 243 of Glycogen [starch] synthase, muscle

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 Glycogen [starch] synthase, muscle between cysteines 189 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
8cvz
Structure name
human glycogenin-1 and glycogen synthase-1 complex in the apo ordered state
Structure deposition date
2022-05-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
100
Peptide accession
P13807
Residue number A
189
Residue number B
243
Peptide name
Glycogen [starch] synthase, muscle

Ligandability

Cysteine 189 of Glycogen [starch] synthase, muscle

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 243 of Glycogen [starch] synthase, muscle

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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