ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phosphotransferase

Intramolecular
Cysteine 233 and cysteine 252
Cysteine 213 and cysteine 220
Cysteine 230 and cysteine 382
Cysteine 220 and cysteine 233
Cysteine 213 and cysteine 233
Cysteine 220 and cysteine 252
A redox-regulated disulphide may form within Phosphotransferase between cysteines 233 and 252.

Details

Redox score ?
69
PDB code
3imx
Structure name
crystal structure of human glucokinase in complex with a synthetic activator
Structure deposition date
2009-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
100
Peptide accession
Q53Y25
Residue number A
233
Residue number B
252
Peptide name
Phosphotransferase

Ligandability

Cysteine 233 of Phosphotransferase

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 Phosphotransferase

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 Phosphotransferase between cysteines 213 and 220.

Details

Redox score ?
67
PDB code
3imx
Structure name
crystal structure of human glucokinase in complex with a synthetic activator
Structure deposition date
2009-08-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
89
Peptide accession
Q53Y25
Residue number A
213
Residue number B
220
Peptide name
Phosphotransferase

Ligandability

Cysteine 213 of Phosphotransferase

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 220 of Phosphotransferase

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 Phosphotransferase between cysteines 230 and 382.

Details

Redox score ?
64
PDB code
3imx
Structure name
crystal structure of human glucokinase in complex with a synthetic activator
Structure deposition date
2009-08-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
Q53Y25
Residue number A
230
Residue number B
382
Peptide name
Phosphotransferase

Ligandability

Cysteine 230 of Phosphotransferase

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 382 of Phosphotransferase

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 Phosphotransferase between cysteines 220 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3imx
Structure name
crystal structure of human glucokinase in complex with a synthetic activator
Structure deposition date
2009-08-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
100
Peptide accession
Q53Y25
Residue number A
220
Residue number B
233
Peptide name
Phosphotransferase

Ligandability

Cysteine 220 of Phosphotransferase

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 233 of Phosphotransferase

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 Phosphotransferase between cysteines 213 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3imx
Structure name
crystal structure of human glucokinase in complex with a synthetic activator
Structure deposition date
2009-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
89
Peptide accession
Q53Y25
Residue number A
213
Residue number B
233
Peptide name
Phosphotransferase

Ligandability

Cysteine 213 of Phosphotransferase

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 233 of Phosphotransferase

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 Phosphotransferase between cysteines 220 and 252. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
3imx
Structure name
crystal structure of human glucokinase in complex with a synthetic activator
Structure deposition date
2009-08-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
17
% buried
100
Peptide accession
Q53Y25
Residue number A
220
Residue number B
252
Peptide name
Phosphotransferase

Ligandability

Cysteine 220 of Phosphotransferase

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 Phosphotransferase

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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