ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Intramolecular
Cysteine 387 and cysteine 412
Cysteine 252 and cysteine 387
Cysteine 394 and cysteine 412
Cysteine 387 and cysteine 394
A redox-regulated disulphide may form within 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 between cysteines 387 and 412 (386 and 411 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
3qpw
Structure name
pfkfb3 in complex with aluminum tetrafluoride
Structure deposition date
2011-02-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
90
Peptide accession
Q16875
Residue number A
387
Residue number B
412
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Ligandability

Cysteine 387 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 412 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 3 between cysteines 252 and 387 (251 and 386 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6etj
Structure name
human pfkfb3 in complex with kan0438241
Structure deposition date
2017-10-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
Q16875
Residue number A
252
Residue number B
387
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Ligandability

Cysteine 252 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 387 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 3 between cysteines 394 and 412 (393 and 411 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5ajv
Structure name
human pfkfb3 in complex with an indole inhibitor 1
Structure deposition date
2015-02-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
98
Peptide accession
Q16875
Residue number A
394
Residue number B
412
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Ligandability

Cysteine 394 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 412 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 3 between cysteines 387 and 394 (386 and 393 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
6ic0
Structure name
human pfkfb3 in complex with a n-aryl 6-aminoquinoxaline inhibitor 4
Structure deposition date
2018-12-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
Q16875
Residue number A
387
Residue number B
394
Peptide name
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Ligandability

Cysteine 387 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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 394 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

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: