ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glycogen phosphorylase, muscle form

Intramolecular
Cysteine 143 and cysteine 496
Cysteine 373 and cysteine 446
A redox-regulated disulphide may form within Glycogen phosphorylase, muscle form between cysteines 143 and 496 (142 and 495 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1gpa
Structure name
structural mechanism for glycogen phosphorylase control by phosphorylation and amp
Structure deposition date
1990-11-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
100
Peptide accession
P00489
Residue number A
143
Residue number B
496
Peptide name
Glycogen phosphorylase, muscle form

Ligandability

Cysteine 143 of Glycogen phosphorylase, muscle form

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 496 of Glycogen phosphorylase, muscle form

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 phosphorylase, muscle form between cysteines 373 and 446 (372 and 445 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3e3o
Structure name
glycogen phosphorylase r state-imp complex
Structure deposition date
2008-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
P00489
Residue number A
373
Residue number B
446
Peptide name
Glycogen phosphorylase, muscle form

Ligandability

Cysteine 373 of Glycogen phosphorylase, muscle form

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 446 of Glycogen phosphorylase, muscle form

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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