ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent 6-phosphofructokinase, muscle type

Intramolecular
Cysteine 550 and cysteine 553
Cysteine 170 and cysteine 212
Cysteine 334 and cysteine 351
Cysteine 170 and cysteine 351
Cysteine 114 and cysteine 334
A redox-regulated disulphide may form within ATP-dependent 6-phosphofructokinase, muscle type between cysteines 550 and 553. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4omt
Structure name
crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Structure deposition date
2014-01-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
96
Peptide accession
P08237
Residue number A
550
Residue number B
553
Peptide name
ATP-dependent 6-phosphofructokinase, muscle type

Ligandability

Cysteine 550 of ATP-dependent 6-phosphofructokinase, muscle 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 553 of ATP-dependent 6-phosphofructokinase, muscle 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, muscle 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 ?
40
PDB code
4omt
Structure name
crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Structure deposition date
2014-01-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
90
Peptide accession
P08237
Residue number A
170
Residue number B
212
Peptide name
ATP-dependent 6-phosphofructokinase, muscle type

Ligandability

Cysteine 170 of ATP-dependent 6-phosphofructokinase, muscle 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, muscle 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, muscle type between cysteines 334 and 351. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3o8l
Structure name
structure of phosphofructokinase from rabbit skeletal muscle
Structure deposition date
2010-08-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
60
Peptide accession
P00511
Residue number A
334
Residue number B
351
Peptide name
ATP-dependent 6-phosphofructokinase, muscle type

Ligandability

Cysteine 334 of ATP-dependent 6-phosphofructokinase, muscle 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, muscle 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, muscle 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 ?
38
PDB code
4omt
Structure name
crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Structure deposition date
2014-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
72
Peptide accession
P08237
Residue number A
170
Residue number B
351
Peptide name
ATP-dependent 6-phosphofructokinase, muscle type

Ligandability

Cysteine 170 of ATP-dependent 6-phosphofructokinase, muscle 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, muscle 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, muscle 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 ?
29
PDB code
4omt
Structure name
crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Structure deposition date
2014-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
11
% buried
86
Peptide accession
P08237
Residue number A
114
Residue number B
334
Peptide name
ATP-dependent 6-phosphofructokinase, muscle type

Ligandability

Cysteine 114 of ATP-dependent 6-phosphofructokinase, muscle 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, muscle 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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