ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ketohexokinase

Intramolecular
Cysteine 8 and cysteine 47
Cysteine 47 and cysteine 57
Cysteine 8 and cysteine 57
Cysteine 98 and cysteine 99
Cysteine 96 and cysteine 98
A redox-regulated disulphide may form within Ketohexokinase between cysteines 8 and 47.

Details

Redox score ?
63
PDB code
6p2d
Structure name
structure of mouse ketohexokinase-c in complex with fructose and adp
Structure deposition date
2019-05-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
99
Minimum pKa ?
10
% buried
100
Peptide accession
A0A0J9YU79
Residue number A
8
Residue number B
47
Peptide name
Ketohexokinase

Ligandability

Cysteine 8 of Ketohexokinase

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 47 of Ketohexokinase

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 Ketohexokinase between cysteines 47 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6p2d
Structure name
structure of mouse ketohexokinase-c in complex with fructose and adp
Structure deposition date
2019-05-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
14
% buried
98
Peptide accession
A0A0J9YU79
Residue number A
47
Residue number B
57
Peptide name
Ketohexokinase

Ligandability

Cysteine 47 of Ketohexokinase

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 57 of Ketohexokinase

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 Ketohexokinase between cysteines 8 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6p2d
Structure name
structure of mouse ketohexokinase-c in complex with fructose and adp
Structure deposition date
2019-05-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
10
% buried
98
Peptide accession
A0A0J9YU79
Residue number A
8
Residue number B
57
Peptide name
Ketohexokinase

Ligandability

Cysteine 8 of Ketohexokinase

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 57 of Ketohexokinase

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 Ketohexokinase between cysteines 98 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6p2d
Structure name
structure of mouse ketohexokinase-c in complex with fructose and adp
Structure deposition date
2019-05-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
44
Peptide accession
A0A0J9YU79
Residue number A
98
Residue number B
99
Peptide name
Ketohexokinase

Ligandability

Cysteine 98 of Ketohexokinase

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 Ketohexokinase

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 Ketohexokinase between cysteines 96 and 98. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
6p2d
Structure name
structure of mouse ketohexokinase-c in complex with fructose and adp
Structure deposition date
2019-05-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
28
Peptide accession
A0A0J9YU79
Residue number A
96
Residue number B
98
Peptide name
Ketohexokinase

Ligandability

Cysteine 96 of Ketohexokinase

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 98 of Ketohexokinase

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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