ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Intramolecular
Cysteine 392 and cysteine 417
Cysteine 257 and cysteine 392
Cysteine 399 and cysteine 417
Cysteine 392 and cysteine 399
A redox-regulated disulphide may form within 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 between cysteines 392 and 417 (391 and 416 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1k6m
Structure name
crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase
Structure deposition date
2001-10-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
100
Peptide accession
P16118
Residue number A
392
Residue number B
417
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Ligandability

Cysteine 392 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 417 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 1 between cysteines 257 and 392 (256 and 391 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1k6m
Structure name
crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase
Structure deposition date
2001-10-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
P16118
Residue number A
257
Residue number B
392
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Ligandability

Cysteine 257 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 392 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 1 between cysteines 399 and 417 (149 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1c7z
Structure name
regulatory complex of fructose-2,6-bisphosphatase
Structure deposition date
2000-04-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
98
Peptide accession
P07953
Residue number A
399
Residue number B
417
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Ligandability

Cysteine 399 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 417 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 1 between cysteines 392 and 399 (391 and 398 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
1k6m
Structure name
crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase
Structure deposition date
2001-10-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
P16118
Residue number A
392
Residue number B
399
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Ligandability

Cysteine 392 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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 399 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

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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