ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

ATP-dependent 6-phosphofructokinase, liver type

Intramolecular
Cysteine 170 and cysteine 212
Cysteine 522 and cysteine 708 L
Cysteine 170 and cysteine 351 L
Cysteine 114 and cysteine 334
A redox-regulated disulphide may form within ATP-dependent 6-phosphofructokinase, liver type between cysteines 170 and 212. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7lw1
Structure name
human phosphofructokinase-1 liver type bound to activator na-11
Structure deposition date
2021-02-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
92
Peptide accession
P17858
Residue number A
170
Residue number B
212
Peptide name
ATP-dependent 6-phosphofructokinase, liver type

Ligandability

Cysteine 170 of ATP-dependent 6-phosphofructokinase, liver type

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 212 of ATP-dependent 6-phosphofructokinase, liver type

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 ATP-dependent 6-phosphofructokinase, liver type between cysteines 522 and 708. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7lw1
Structure name
human phosphofructokinase-1 liver type bound to activator na-11
Structure deposition date
2021-02-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
11
% buried
84
Peptide accession
P17858
Residue number A
522
Residue number B
708
Peptide name
ATP-dependent 6-phosphofructokinase, liver type

Ligandability

Cysteine 522 of ATP-dependent 6-phosphofructokinase, liver type

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 708 of ATP-dependent 6-phosphofructokinase, liver type

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within ATP-dependent 6-phosphofructokinase, liver type between cysteines 170 and 351. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7lw1
Structure name
human phosphofructokinase-1 liver type bound to activator na-11
Structure deposition date
2021-02-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
70
Peptide accession
P17858
Residue number A
170
Residue number B
351
Peptide name
ATP-dependent 6-phosphofructokinase, liver type

Ligandability

Cysteine 170 of ATP-dependent 6-phosphofructokinase, liver type

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 351 of ATP-dependent 6-phosphofructokinase, liver type

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.

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 ATP-dependent 6-phosphofructokinase, liver type between cysteines 114 and 334. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7lw1
Structure name
human phosphofructokinase-1 liver type bound to activator na-11
Structure deposition date
2021-02-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
88
Peptide accession
P17858
Residue number A
114
Residue number B
334
Peptide name
ATP-dependent 6-phosphofructokinase, liver type

Ligandability

Cysteine 114 of ATP-dependent 6-phosphofructokinase, liver type

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 334 of ATP-dependent 6-phosphofructokinase, liver type

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.

If this tool was useful for finding a disulphide, please cite: