ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Intramolecular
Cysteine 390 and cysteine 415
Cysteine 255 and cysteine 390
Cysteine 397 and cysteine 415
Cysteine 390 and cysteine 397
A redox-regulated disulphide may form within 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 between cysteines 390 and 415 (389 and 414 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1bif
Structure name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase bifunctional enzyme complexed with atp-g-s and phosphate
Structure deposition date
1996-11-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
100
Peptide accession
P25114
Residue number A
390
Residue number B
415
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Ligandability

Cysteine 390 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 415 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 between cysteines 255 and 390 (254 and 389 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2bif
Structure name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase h256a mutant with f6p in phosphatase active site
Structure deposition date
1998-10-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
P25114
Residue number A
255
Residue number B
390
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Ligandability

Cysteine 255 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 390 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 between cysteines 397 and 415 (396 and 414 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2bif
Structure name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase h256a mutant with f6p in phosphatase active site
Structure deposition date
1998-10-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
100
Peptide accession
P25114
Residue number A
397
Residue number B
415
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Ligandability

Cysteine 397 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 415 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 between cysteines 390 and 397 (389 and 396 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
2bif
Structure name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase h256a mutant with f6p in phosphatase active site
Structure deposition date
1998-10-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
13
% buried
100
Peptide accession
P25114
Residue number A
390
Residue number B
397
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Ligandability

Cysteine 390 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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 397 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

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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