ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Intramolecular
Cysteine 435 and cysteine 454
Cysteine 384 and cysteine 435
Cysteine 384 and cysteine 478
Cysteine 570 and cysteine 620
Cysteine 511 and cysteine 661
A redox-regulated disulphide may form within Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 between cysteines 435 and 454.

Details

Redox score ?
70
PDB code
2v4m
Structure name
the isomerase domain of human glutamine-fructose-6-phosphate transaminase 1 (gfpt1) in complex with fructose 6-phosphate
Structure deposition date
2008-09-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
99
Peptide accession
Q06210
Residue number A
435
Residue number B
454
Peptide name
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Ligandability

Cysteine 435 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 454 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 between cysteines 384 and 435 (366 and 417 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
6svq
Structure name
crystal structure of human gfat-1 g461e after udp-glcnac soaking
Structure deposition date
2019-09-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
72
Peptide accession
Q06210
Residue number A
384
Residue number B
435
Peptide name
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Ligandability

Cysteine 384 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 435 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 between cysteines 384 and 478 (366 and 460 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6svp
Structure name
crystal structure of human gfat-1 in complex with glucose-6-phosphate, l-glu, and udp-glcnac
Structure deposition date
2019-09-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
60
Peptide accession
Q06210
Residue number A
384
Residue number B
478
Peptide name
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Ligandability

Cysteine 384 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 478 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 between cysteines 570 and 620 (552 and 602 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6svp
Structure name
crystal structure of human gfat-1 in complex with glucose-6-phosphate, l-glu, and udp-glcnac
Structure deposition date
2019-09-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q06210
Residue number A
570
Residue number B
620
Peptide name
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Ligandability

Cysteine 570 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 620 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 between cysteines 511 and 661 (493 and 643 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
6r4i
Structure name
crystal structure of human gfat-1 g461e
Structure deposition date
2019-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
80
Peptide accession
Q06210
Residue number A
511
Residue number B
661
Peptide name
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Ligandability

Cysteine 511 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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 661 of Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 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.

If this tool was useful for finding a disulphide, please cite: