ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent 6-phosphofructokinase, platelet type

Intramolecular
Cysteine 343 and cysteine 360
Cysteine 179 and cysteine 360 L
Cysteine 179 and cysteine 221 L
Cysteine 123 and cysteine 343 L
A redox-regulated disulphide may form within ATP-dependent 6-phosphofructokinase, platelet type between cysteines 343 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4wl0
Structure name
ligand-free structure of human platelet phosphofructokinase in an r- state, crystal form i
Structure deposition date
2014-10-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
46
Peptide accession
Q01813
Residue number A
343
Residue number B
360
Peptide name
ATP-dependent 6-phosphofructokinase, platelet type

Ligandability

Cysteine 343 of ATP-dependent 6-phosphofructokinase, platelet 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 360 of ATP-dependent 6-phosphofructokinase, platelet 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, platelet type between cysteines 179 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4u1r
Structure name
atp-bound structure of human platelet phosphofructokinase in an r- state, crystal form ii
Structure deposition date
2014-07-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
66
Peptide accession
Q01813
Residue number A
179
Residue number B
360
Peptide name
ATP-dependent 6-phosphofructokinase, platelet type

Ligandability

Cysteine 179 of ATP-dependent 6-phosphofructokinase, platelet type

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 360 of ATP-dependent 6-phosphofructokinase, platelet 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, platelet type between cysteines 179 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4rh3
Structure name
amppcp-bound structure of human platelet phosphofructokinase in an r- state, crystal form ii
Structure deposition date
2014-10-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
86
Peptide accession
Q01813
Residue number A
179
Residue number B
221
Peptide name
ATP-dependent 6-phosphofructokinase, platelet type

Ligandability

Cysteine 179 of ATP-dependent 6-phosphofructokinase, platelet type

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 221 of ATP-dependent 6-phosphofructokinase, platelet 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, platelet type between cysteines 123 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
4u1r
Structure name
atp-bound structure of human platelet phosphofructokinase in an r- state, crystal form ii
Structure deposition date
2014-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
88
Peptide accession
Q01813
Residue number A
123
Residue number B
343
Peptide name
ATP-dependent 6-phosphofructokinase, platelet type

Ligandability

Cysteine 123 of ATP-dependent 6-phosphofructokinase, platelet 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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 343 of ATP-dependent 6-phosphofructokinase, platelet 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.

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