ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutaminase kidney isoform, mitochondrial

Intramolecular
Cysteine 505 and cysteine 523 L
Cysteine 183 and cysteine 208 L
Cysteine 271 and cysteine 445 L
Cysteine 287 and cysteine 500
Cysteine 429 and cysteine 505
Cysteine 288 and cysteine 423
Cysteine 292 and cysteine 423
Cysteine 287 and cysteine 424
A redox-regulated disulphide may form within Glutaminase kidney isoform, mitochondrial between cysteines 505 and 523.

Details

Redox score ?
60
PDB code
3ss4
Structure name
crystal structure of mouse glutaminase c, phosphate-bound form
Structure deposition date
2011-07-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
102
Minimum pKa ?
9
% buried
100
Peptide accession
Q69ZX9
Residue number A
505
Residue number B
523
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 505 of Glutaminase kidney isoform, mitochondrial

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 523 of Glutaminase kidney isoform, mitochondrial

Not ligandable in the dataset of Yang et al.

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 Glutaminase kidney isoform, mitochondrial between cysteines 183 and 208. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3ss4
Structure name
crystal structure of mouse glutaminase c, phosphate-bound form
Structure deposition date
2011-07-07
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
57
Peptide accession
Q69ZX9
Residue number A
183
Residue number B
208
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 183 of Glutaminase kidney isoform, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 208 of Glutaminase kidney isoform, mitochondrial

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 Glutaminase kidney isoform, mitochondrial between cysteines 271 and 445. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3ss5
Structure name
crystal structure of mouse glutaminase c, l-glutamate-bound form
Structure deposition date
2011-07-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
92
Peptide accession
Q69ZX9
Residue number A
271
Residue number B
445
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 271 of Glutaminase kidney isoform, mitochondrial

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 445 of Glutaminase kidney isoform, mitochondrial

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 Glutaminase kidney isoform, mitochondrial between cysteines 287 and 500. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
5uqe
Structure name
multidomain structure of human kidney-type glutaminase(kga/gls)
Structure deposition date
2017-02-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
7
% buried
100
Peptide accession
O94925
Residue number A
287
Residue number B
500
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 287 of Glutaminase kidney isoform, mitochondrial

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 500 of Glutaminase kidney isoform, mitochondrial

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 Glutaminase kidney isoform, mitochondrial between cysteines 429 and 505. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3ss3
Structure name
crystal structure of mouse glutaminase c, ligand-free form
Structure deposition date
2011-07-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
102
Minimum pKa ?
13
% buried
100
Peptide accession
Q69ZX9
Residue number A
429
Residue number B
505
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 429 of Glutaminase kidney isoform, mitochondrial

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 505 of Glutaminase kidney isoform, mitochondrial

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 Glutaminase kidney isoform, mitochondrial between cysteines 288 and 423. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3ss5
Structure name
crystal structure of mouse glutaminase c, l-glutamate-bound form
Structure deposition date
2011-07-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
10
% buried
96
Peptide accession
Q69ZX9
Residue number A
288
Residue number B
423
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 288 of Glutaminase kidney isoform, mitochondrial

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 423 of Glutaminase kidney isoform, mitochondrial

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 Glutaminase kidney isoform, mitochondrial between cysteines 292 and 423. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4jkt
Structure name
crystal structure of mouse glutaminase c, bptes-bound form
Structure deposition date
2013-03-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
10
% buried
100
Peptide accession
D3Z7P3
Residue number A
292
Residue number B
423
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 292 of Glutaminase kidney isoform, mitochondrial

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 423 of Glutaminase kidney isoform, mitochondrial

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 Glutaminase kidney isoform, mitochondrial between cysteines 287 and 424. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6ul9
Structure name
crystal structure of human gac in complex with inhibitor upgl00023
Structure deposition date
2019-10-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
99
Minimum pKa ?
11
% buried
100
Peptide accession
O94925
Residue number A
287
Residue number B
424
Peptide name
Glutaminase kidney isoform, mitochondrial

Ligandability

Cysteine 287 of Glutaminase kidney isoform, mitochondrial

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 424 of Glutaminase kidney isoform, mitochondrial

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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